ADH1E_HORSE
ID ADH1E_HORSE Reviewed; 375 AA.
AC P00327;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Alcohol dehydrogenase E chain;
DE EC=1.1.1.1;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=1712777; DOI=10.1016/s0021-9258(18)98838-1;
RA Park D.H., Plapp B.V.;
RT "Isoenzymes of horse liver alcohol dehydrogenase active on ethanol and
RT steroids. cDNA cloning, expression, and comparison of active sites.";
RL J. Biol. Chem. 266:13296-13302(1991).
RN [2]
RP PROTEIN SEQUENCE OF 2-375, AND ACETYLATION AT SER-2.
RC TISSUE=Liver;
RX PubMed=5466062; DOI=10.1111/j.1432-1033.1970.tb01050.x;
RA Joernvall H.;
RT "Horse liver alcohol dehydrogenase. On the primary structures of the
RT isoenzymes.";
RL Eur. J. Biochem. 16:41-49(1970).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=178875; DOI=10.1016/0022-2836(76)90072-3;
RA Eklund H., Nordstroem B., Zeppezauer E., Soederlund G., Ohlsson I.,
RA Boiwe T., Soederberg B.-O., Tapia O., Braenden C.-I., Aakeson A.;
RT "Three-dimensional structure of horse liver alcohol dehydrogenase at 2.4-A
RT resolution.";
RL J. Mol. Biol. 102:27-59(1976).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
RX PubMed=6098306; DOI=10.1021/bi00320a014;
RA Eklund H., Samama J.-P., Jones T.A.;
RT "Crystallographic investigations of nicotinamide adenine dinucleotide
RT binding to horse liver alcohol dehydrogenase.";
RL Biochemistry 23:5982-5996(1984).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 2-375 IN COMPLEX WITH NAD AND
RP ZINC, AND COFACTOR.
RX PubMed=15299346; DOI=10.1107/s0907444994005263;
RA Al-Karadaghi S., Cedergren-Zeppezauer E.S., Hovmoeller S., Petratos K.,
RA Terry H., Wilson K.S.;
RT "Refined crystal structure of liver alcohol dehydrogenase-NADH complex at
RT 1.8-A resolution.";
RL Acta Crystallogr. D 50:793-807(1994).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH;
CC Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a secondary alcohol + NAD(+) = a ketone + H(+) + NADH;
CC Xref=Rhea:RHEA:10740, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087,
CC ChEBI:CHEBI:35681, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:15299346};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:15299346};
CC -!- SUBUNIT: Dimer of identical or non-identical chains of two types (E and
CC S) coded by 2 separate genes at different loci.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Class-I subfamily. {ECO:0000305}.
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DR EMBL; M64864; AAA30931.1; -; mRNA.
DR PIR; A39872; DEHOAL.
DR RefSeq; NP_001075997.1; NM_001082528.1.
DR PDB; 1A71; X-ray; 2.00 A; A/B=2-375.
DR PDB; 1A72; X-ray; 2.60 A; A=2-375.
DR PDB; 1ADB; X-ray; 2.40 A; A/B=2-375.
DR PDB; 1ADC; X-ray; 2.70 A; A/B=2-375.
DR PDB; 1ADF; X-ray; 2.90 A; A=2-375.
DR PDB; 1ADG; X-ray; 2.70 A; A=2-375.
DR PDB; 1AXE; X-ray; 2.00 A; A/B=2-375.
DR PDB; 1AXG; X-ray; 2.50 A; A/B/C/D=2-375.
DR PDB; 1BTO; X-ray; 2.00 A; A/B/C/D=2-375.
DR PDB; 1HET; X-ray; 1.15 A; A/B=2-375.
DR PDB; 1HEU; X-ray; 1.15 A; A/B=2-375.
DR PDB; 1HF3; X-ray; 1.95 A; A/B=2-375.
DR PDB; 1HLD; X-ray; 2.10 A; A/B=2-375.
DR PDB; 1JU9; X-ray; 2.00 A; A/B=2-375.
DR PDB; 1LDE; X-ray; 2.50 A; A/B/C/D=2-375.
DR PDB; 1LDY; X-ray; 2.50 A; A/B/C/D=2-375.
DR PDB; 1MG0; X-ray; 1.80 A; A/B/C/D=2-375.
DR PDB; 1MGO; X-ray; 1.20 A; A/B=2-375.
DR PDB; 1N8K; X-ray; 1.13 A; A/B=2-375.
DR PDB; 1N92; X-ray; 1.47 A; A/B=2-375.
DR PDB; 1P1R; X-ray; 1.57 A; A/B/C/D=2-375.
DR PDB; 1QLH; X-ray; 2.07 A; A=2-375.
DR PDB; 1QLJ; X-ray; 2.80 A; A=2-375.
DR PDB; 1QV6; X-ray; 1.80 A; A/B=2-375.
DR PDB; 1QV7; X-ray; 1.80 A; A/B=2-375.
DR PDB; 1YE3; X-ray; 1.59 A; A=2-375.
DR PDB; 2JHF; X-ray; 1.00 A; A/B=2-375.
DR PDB; 2JHG; X-ray; 1.20 A; A/B=2-375.
DR PDB; 2OHX; X-ray; 1.80 A; A/B=2-375.
DR PDB; 2OXI; X-ray; 2.10 A; A/B=2-375.
DR PDB; 3BTO; X-ray; 1.66 A; A/B/C/D=2-375.
DR PDB; 3OQ6; X-ray; 1.20 A; A/B=2-375.
DR PDB; 4DWV; X-ray; 1.14 A; A/B=2-375.
DR PDB; 4DXH; X-ray; 1.12 A; A/B=2-375.
DR PDB; 4NFH; X-ray; 1.20 A; A/B=2-375.
DR PDB; 4NFS; X-ray; 1.10 A; A/B=2-375.
DR PDB; 4NG5; X-ray; 1.10 A; A/B=2-375.
DR PDB; 4XD2; X-ray; 1.10 A; A/B=2-375.
DR PDB; 5ADH; X-ray; 2.90 A; A=2-375.
DR PDB; 5CDG; X-ray; 1.40 A; A/B=2-375.
DR PDB; 5CDS; X-ray; 1.40 A; A/B=2-375.
DR PDB; 5CDT; X-ray; 1.70 A; A/B=2-375.
DR PDB; 5CDU; X-ray; 1.60 A; A/B=2-375.
DR PDB; 5KCP; X-ray; 1.10 A; A/B=2-375.
DR PDB; 5KCZ; X-ray; 1.14 A; A/B=2-375.
DR PDB; 5KJ1; X-ray; 1.20 A; A/B=2-375.
DR PDB; 5KJ6; X-ray; 1.14 A; A/B=2-375.
DR PDB; 5KJC; X-ray; 1.20 A; A/B=2-375.
DR PDB; 5KJE; X-ray; 1.26 A; A/B=2-375.
DR PDB; 5KJF; X-ray; 1.20 A; A/B=2-375.
DR PDB; 5VJ5; X-ray; 1.90 A; A/B=2-375.
DR PDB; 5VJG; X-ray; 1.90 A; A=2-375.
DR PDB; 5VKR; X-ray; 1.80 A; A=2-375.
DR PDB; 5VL0; X-ray; 1.20 A; A/B/C/D=2-375.
DR PDB; 5VN1; X-ray; 1.25 A; A/B/C/D=2-375.
DR PDB; 6ADH; X-ray; 2.90 A; A/B=2-375.
DR PDB; 6CXX; X-ray; 1.26 A; A/B=2-375.
DR PDB; 6CY3; X-ray; 2.30 A; A=2-375.
DR PDB; 6NBB; EM; 2.90 A; A/B=2-375.
DR PDB; 6O91; X-ray; 1.10 A; A/B=2-375.
DR PDB; 6OA7; X-ray; 1.10 A; A/B=2-375.
DR PDB; 6OWM; X-ray; 1.10 A; A/B=2-375.
DR PDB; 6OWP; X-ray; 1.14 A; A/B=2-375.
DR PDB; 6XT2; X-ray; 1.55 A; A/B/C/D=2-375.
DR PDB; 7ADH; X-ray; 3.20 A; A=2-375.
DR PDB; 7JQA; X-ray; 1.53 A; A/B/C/D=2-375.
DR PDB; 7K35; X-ray; 1.20 A; A/B/C/D=2-375.
DR PDB; 7UA6; X-ray; 1.10 A; A/B=2-375.
DR PDB; 7UC9; X-ray; 1.10 A; A/B=2-375.
DR PDB; 7UCA; X-ray; 1.10 A; A/B=2-375.
DR PDB; 7UCU; X-ray; 1.10 A; A/B=2-375.
DR PDB; 7UDD; X-ray; 1.10 A; A/B=2-375.
DR PDB; 7UDE; X-ray; 1.10 A; A/B=2-375.
DR PDB; 7UDR; X-ray; 1.20 A; A/B=2-375.
DR PDB; 7UEC; X-ray; 1.20 A; A/B=2-375.
DR PDB; 7UEE; X-ray; 1.20 A; A/B=2-375.
DR PDB; 7UEF; X-ray; 1.20 A; A/B=2-375.
DR PDB; 7UEI; X-ray; 1.20 A; A/B=2-375.
DR PDB; 7UEJ; X-ray; 1.20 A; A/B=2-375.
DR PDB; 7UHV; X-ray; 1.30 A; A/B=2-375.
DR PDB; 7UHW; X-ray; 1.30 A; A/B=2-375.
DR PDB; 7UHX; X-ray; 1.30 A; A/B=2-375.
DR PDB; 8ADH; X-ray; 2.40 A; A=2-375.
DR PDBsum; 1A71; -.
DR PDBsum; 1A72; -.
DR PDBsum; 1ADB; -.
DR PDBsum; 1ADC; -.
DR PDBsum; 1ADF; -.
DR PDBsum; 1ADG; -.
DR PDBsum; 1AXE; -.
DR PDBsum; 1AXG; -.
DR PDBsum; 1BTO; -.
DR PDBsum; 1HET; -.
DR PDBsum; 1HEU; -.
DR PDBsum; 1HF3; -.
DR PDBsum; 1HLD; -.
DR PDBsum; 1JU9; -.
DR PDBsum; 1LDE; -.
DR PDBsum; 1LDY; -.
DR PDBsum; 1MG0; -.
DR PDBsum; 1MGO; -.
DR PDBsum; 1N8K; -.
DR PDBsum; 1N92; -.
DR PDBsum; 1P1R; -.
DR PDBsum; 1QLH; -.
DR PDBsum; 1QLJ; -.
DR PDBsum; 1QV6; -.
DR PDBsum; 1QV7; -.
DR PDBsum; 1YE3; -.
DR PDBsum; 2JHF; -.
DR PDBsum; 2JHG; -.
DR PDBsum; 2OHX; -.
DR PDBsum; 2OXI; -.
DR PDBsum; 3BTO; -.
DR PDBsum; 3OQ6; -.
DR PDBsum; 4DWV; -.
DR PDBsum; 4DXH; -.
DR PDBsum; 4NFH; -.
DR PDBsum; 4NFS; -.
DR PDBsum; 4NG5; -.
DR PDBsum; 4XD2; -.
DR PDBsum; 5ADH; -.
DR PDBsum; 5CDG; -.
DR PDBsum; 5CDS; -.
DR PDBsum; 5CDT; -.
DR PDBsum; 5CDU; -.
DR PDBsum; 5KCP; -.
DR PDBsum; 5KCZ; -.
DR PDBsum; 5KJ1; -.
DR PDBsum; 5KJ6; -.
DR PDBsum; 5KJC; -.
DR PDBsum; 5KJE; -.
DR PDBsum; 5KJF; -.
DR PDBsum; 5VJ5; -.
DR PDBsum; 5VJG; -.
DR PDBsum; 5VKR; -.
DR PDBsum; 5VL0; -.
DR PDBsum; 5VN1; -.
DR PDBsum; 6ADH; -.
DR PDBsum; 6CXX; -.
DR PDBsum; 6CY3; -.
DR PDBsum; 6NBB; -.
DR PDBsum; 6O91; -.
DR PDBsum; 6OA7; -.
DR PDBsum; 6OWM; -.
DR PDBsum; 6OWP; -.
DR PDBsum; 6XT2; -.
DR PDBsum; 7ADH; -.
DR PDBsum; 7JQA; -.
DR PDBsum; 7K35; -.
DR PDBsum; 7UA6; -.
DR PDBsum; 7UC9; -.
DR PDBsum; 7UCA; -.
DR PDBsum; 7UCU; -.
DR PDBsum; 7UDD; -.
DR PDBsum; 7UDE; -.
DR PDBsum; 7UDR; -.
DR PDBsum; 7UEC; -.
DR PDBsum; 7UEE; -.
DR PDBsum; 7UEF; -.
DR PDBsum; 7UEI; -.
DR PDBsum; 7UEJ; -.
DR PDBsum; 7UHV; -.
DR PDBsum; 7UHW; -.
DR PDBsum; 7UHX; -.
DR PDBsum; 8ADH; -.
DR AlphaFoldDB; P00327; -.
DR SMR; P00327; -.
DR STRING; 9796.ENSECAP00000033917; -.
DR BindingDB; P00327; -.
DR ChEMBL; CHEMBL2111372; -.
DR DrugCentral; P00327; -.
DR iPTMnet; P00327; -.
DR PaxDb; P00327; -.
DR PeptideAtlas; P00327; -.
DR GeneID; 100034242; -.
DR KEGG; ecb:100034242; -.
DR OrthoDB; 664798at2759; -.
DR BRENDA; 1.1.1.1; 2120.
DR SABIO-RK; P00327; -.
DR EvolutionaryTrace; P00327; -.
DR PRO; PR:P00327; -.
DR Proteomes; UP000002281; Unplaced.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004024; F:alcohol dehydrogenase activity, zinc-dependent; IBA:GO_Central.
DR GO; GO:0004745; F:NAD-retinol dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0006069; P:ethanol oxidation; IBA:GO_Central.
DR GO; GO:0042573; P:retinoic acid metabolic process; IBA:GO_Central.
DR GO; GO:0042572; P:retinol metabolic process; IBA:GO_Central.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 2.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Metal-binding; NAD; Oxidoreductase; Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:5466062"
FT CHAIN 2..375
FT /note="Alcohol dehydrogenase E chain"
FT /id="PRO_0000160656"
FT BINDING 47
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:15299346,
FT ECO:0000269|PubMed:178875, ECO:0007744|PDB:1A71,
FT ECO:0007744|PDB:1A72, ECO:0007744|PDB:1ADB,
FT ECO:0007744|PDB:1ADC, ECO:0007744|PDB:1ADF,
FT ECO:0007744|PDB:1ADG, ECO:0007744|PDB:1AXE,
FT ECO:0007744|PDB:1AXG, ECO:0007744|PDB:1BTO,
FT ECO:0007744|PDB:1HET, ECO:0007744|PDB:1HLD,
FT ECO:0007744|PDB:1JU9, ECO:0007744|PDB:1LDE,
FT ECO:0007744|PDB:1LDY, ECO:0007744|PDB:1MG0,
FT ECO:0007744|PDB:1MGO, ECO:0007744|PDB:1N8K,
FT ECO:0007744|PDB:1N92, ECO:0007744|PDB:1P1R,
FT ECO:0007744|PDB:1QLH, ECO:0007744|PDB:1QLJ,
FT ECO:0007744|PDB:1QV6, ECO:0007744|PDB:1QV7,
FT ECO:0007744|PDB:1YE3, ECO:0007744|PDB:2JHG,
FT ECO:0007744|PDB:2OHX, ECO:0007744|PDB:3BTO,
FT ECO:0007744|PDB:3OQ6, ECO:0007744|PDB:4DWV,
FT ECO:0007744|PDB:4DXH, ECO:0007744|PDB:4NFH,
FT ECO:0007744|PDB:4NFS, ECO:0007744|PDB:4NG5,
FT ECO:0007744|PDB:4XD2, ECO:0007744|PDB:5ADH,
FT ECO:0007744|PDB:6ADH, ECO:0007744|PDB:7ADH,
FT ECO:0007744|PDB:8ADH"
FT BINDING 49
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 49
FT /ligand="substrate"
FT /evidence="ECO:0007744|PDB:1A71, ECO:0007744|PDB:1ADC,
FT ECO:0007744|PDB:1AXE, ECO:0007744|PDB:1AXG,
FT ECO:0007744|PDB:1HLD, ECO:0007744|PDB:1MG0,
FT ECO:0007744|PDB:1QV7, ECO:0007744|PDB:3OQ6,
FT ECO:0007744|PDB:4DWV, ECO:0007744|PDB:4DXH,
FT ECO:0007744|PDB:4NFH, ECO:0007744|PDB:4NFS,
FT ECO:0007744|PDB:4NG5"
FT BINDING 49
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 68
FT /ligand="substrate"
FT /evidence="ECO:0007744|PDB:1A71, ECO:0007744|PDB:1ADC,
FT ECO:0007744|PDB:1AXE, ECO:0007744|PDB:1HLD,
FT ECO:0007744|PDB:1MG0, ECO:0007744|PDB:1QV7,
FT ECO:0007744|PDB:3OQ6, ECO:0007744|PDB:4DWV,
FT ECO:0007744|PDB:4DXH, ECO:0007744|PDB:4NFH,
FT ECO:0007744|PDB:4NFS, ECO:0007744|PDB:4NG5"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:15299346,
FT ECO:0000269|PubMed:178875, ECO:0007744|PDB:1A71,
FT ECO:0007744|PDB:1A72, ECO:0007744|PDB:1ADB,
FT ECO:0007744|PDB:1ADC, ECO:0007744|PDB:1ADF,
FT ECO:0007744|PDB:1ADG, ECO:0007744|PDB:1AXE,
FT ECO:0007744|PDB:1AXG, ECO:0007744|PDB:1BTO,
FT ECO:0007744|PDB:1HET, ECO:0007744|PDB:1HLD,
FT ECO:0007744|PDB:1JU9, ECO:0007744|PDB:1LDE,
FT ECO:0007744|PDB:1LDY, ECO:0007744|PDB:1MG0,
FT ECO:0007744|PDB:1MGO, ECO:0007744|PDB:1N8K,
FT ECO:0007744|PDB:1N92, ECO:0007744|PDB:1P1R,
FT ECO:0007744|PDB:1QLH, ECO:0007744|PDB:1QLJ,
FT ECO:0007744|PDB:1QV6, ECO:0007744|PDB:1QV7,
FT ECO:0007744|PDB:1YE3, ECO:0007744|PDB:2JHG,
FT ECO:0007744|PDB:2OHX, ECO:0007744|PDB:3BTO,
FT ECO:0007744|PDB:3OQ6, ECO:0007744|PDB:4DWV,
FT ECO:0007744|PDB:4DXH, ECO:0007744|PDB:4NFH,
FT ECO:0007744|PDB:4NFS, ECO:0007744|PDB:4NG5,
FT ECO:0007744|PDB:4XD2, ECO:0007744|PDB:5ADH,
FT ECO:0007744|PDB:6ADH, ECO:0007744|PDB:7ADH,
FT ECO:0007744|PDB:8ADH"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15299346,
FT ECO:0000269|PubMed:178875, ECO:0007744|PDB:1A71,
FT ECO:0007744|PDB:1A72, ECO:0007744|PDB:1ADB,
FT ECO:0007744|PDB:1ADC, ECO:0007744|PDB:1ADF,
FT ECO:0007744|PDB:1ADG, ECO:0007744|PDB:1AXE,
FT ECO:0007744|PDB:1AXG, ECO:0007744|PDB:1BTO,
FT ECO:0007744|PDB:1HET, ECO:0007744|PDB:1HLD,
FT ECO:0007744|PDB:1JU9, ECO:0007744|PDB:1LDE,
FT ECO:0007744|PDB:1LDY, ECO:0007744|PDB:1MG0,
FT ECO:0007744|PDB:1MGO, ECO:0007744|PDB:1N8K,
FT ECO:0007744|PDB:1N92, ECO:0007744|PDB:1P1R,
FT ECO:0007744|PDB:1QLH, ECO:0007744|PDB:1QLJ,
FT ECO:0007744|PDB:1QV6, ECO:0007744|PDB:1QV7,
FT ECO:0007744|PDB:1YE3, ECO:0007744|PDB:2JHG,
FT ECO:0007744|PDB:2OHX, ECO:0007744|PDB:2OXI,
FT ECO:0007744|PDB:3BTO, ECO:0007744|PDB:3OQ6,
FT ECO:0007744|PDB:4DWV, ECO:0007744|PDB:4DXH,
FT ECO:0007744|PDB:4NFH, ECO:0007744|PDB:4NFS,
FT ECO:0007744|PDB:4NG5, ECO:0007744|PDB:4XD2,
FT ECO:0007744|PDB:5ADH, ECO:0007744|PDB:6ADH,
FT ECO:0007744|PDB:7ADH, ECO:0007744|PDB:8ADH"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15299346,
FT ECO:0000269|PubMed:178875, ECO:0007744|PDB:1A71,
FT ECO:0007744|PDB:1A72, ECO:0007744|PDB:1ADB,
FT ECO:0007744|PDB:1ADC, ECO:0007744|PDB:1ADF,
FT ECO:0007744|PDB:1ADG, ECO:0007744|PDB:1AXE,
FT ECO:0007744|PDB:1AXG, ECO:0007744|PDB:1BTO,
FT ECO:0007744|PDB:1HET, ECO:0007744|PDB:1HLD,
FT ECO:0007744|PDB:1JU9, ECO:0007744|PDB:1LDE,
FT ECO:0007744|PDB:1LDY, ECO:0007744|PDB:1MG0,
FT ECO:0007744|PDB:1MGO, ECO:0007744|PDB:1N8K,
FT ECO:0007744|PDB:1N92, ECO:0007744|PDB:1P1R,
FT ECO:0007744|PDB:1QLH, ECO:0007744|PDB:1QLJ,
FT ECO:0007744|PDB:1QV6, ECO:0007744|PDB:1QV7,
FT ECO:0007744|PDB:1YE3, ECO:0007744|PDB:2JHG,
FT ECO:0007744|PDB:2OHX, ECO:0007744|PDB:2OXI,
FT ECO:0007744|PDB:3BTO, ECO:0007744|PDB:3OQ6,
FT ECO:0007744|PDB:4DWV, ECO:0007744|PDB:4DXH,
FT ECO:0007744|PDB:4NFH, ECO:0007744|PDB:4NFS,
FT ECO:0007744|PDB:4NG5, ECO:0007744|PDB:4XD2,
FT ECO:0007744|PDB:5ADH, ECO:0007744|PDB:6ADH,
FT ECO:0007744|PDB:7ADH, ECO:0007744|PDB:8ADH"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15299346,
FT ECO:0000269|PubMed:178875, ECO:0007744|PDB:1A71,
FT ECO:0007744|PDB:1A72, ECO:0007744|PDB:1ADB,
FT ECO:0007744|PDB:1ADC, ECO:0007744|PDB:1ADF,
FT ECO:0007744|PDB:1ADG, ECO:0007744|PDB:1AXE,
FT ECO:0007744|PDB:1AXG, ECO:0007744|PDB:1BTO,
FT ECO:0007744|PDB:1HET, ECO:0007744|PDB:1HLD,
FT ECO:0007744|PDB:1JU9, ECO:0007744|PDB:1LDE,
FT ECO:0007744|PDB:1LDY, ECO:0007744|PDB:1MG0,
FT ECO:0007744|PDB:1MGO, ECO:0007744|PDB:1N8K,
FT ECO:0007744|PDB:1N92, ECO:0007744|PDB:1P1R,
FT ECO:0007744|PDB:1QLH, ECO:0007744|PDB:1QLJ,
FT ECO:0007744|PDB:1QV6, ECO:0007744|PDB:1QV7,
FT ECO:0007744|PDB:1YE3, ECO:0007744|PDB:2JHG,
FT ECO:0007744|PDB:2OHX, ECO:0007744|PDB:2OXI,
FT ECO:0007744|PDB:3BTO, ECO:0007744|PDB:3OQ6,
FT ECO:0007744|PDB:4DWV, ECO:0007744|PDB:4DXH,
FT ECO:0007744|PDB:4NFH, ECO:0007744|PDB:4NFS,
FT ECO:0007744|PDB:4NG5, ECO:0007744|PDB:4XD2,
FT ECO:0007744|PDB:5ADH, ECO:0007744|PDB:6ADH,
FT ECO:0007744|PDB:7ADH, ECO:0007744|PDB:8ADH"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15299346,
FT ECO:0000269|PubMed:178875, ECO:0007744|PDB:1A71,
FT ECO:0007744|PDB:1A72, ECO:0007744|PDB:1ADB,
FT ECO:0007744|PDB:1ADC, ECO:0007744|PDB:1ADF,
FT ECO:0007744|PDB:1ADG, ECO:0007744|PDB:1AXE,
FT ECO:0007744|PDB:1AXG, ECO:0007744|PDB:1BTO,
FT ECO:0007744|PDB:1HET, ECO:0007744|PDB:1HLD,
FT ECO:0007744|PDB:1JU9, ECO:0007744|PDB:1LDE,
FT ECO:0007744|PDB:1LDY, ECO:0007744|PDB:1MG0,
FT ECO:0007744|PDB:1MGO, ECO:0007744|PDB:1N8K,
FT ECO:0007744|PDB:1N92, ECO:0007744|PDB:1P1R,
FT ECO:0007744|PDB:1QLH, ECO:0007744|PDB:1QLJ,
FT ECO:0007744|PDB:1QV6, ECO:0007744|PDB:1QV7,
FT ECO:0007744|PDB:1YE3, ECO:0007744|PDB:2JHG,
FT ECO:0007744|PDB:2OHX, ECO:0007744|PDB:2OXI,
FT ECO:0007744|PDB:3BTO, ECO:0007744|PDB:3OQ6,
FT ECO:0007744|PDB:4DWV, ECO:0007744|PDB:4DXH,
FT ECO:0007744|PDB:4NFH, ECO:0007744|PDB:4NFS,
FT ECO:0007744|PDB:4NG5, ECO:0007744|PDB:4XD2,
FT ECO:0007744|PDB:5ADH, ECO:0007744|PDB:6ADH,
FT ECO:0007744|PDB:7ADH, ECO:0007744|PDB:8ADH"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:15299346,
FT ECO:0007744|PDB:1A71, ECO:0007744|PDB:1A72,
FT ECO:0007744|PDB:1ADB, ECO:0007744|PDB:1ADC,
FT ECO:0007744|PDB:1ADF, ECO:0007744|PDB:1ADG,
FT ECO:0007744|PDB:1AXE, ECO:0007744|PDB:1AXG,
FT ECO:0007744|PDB:1BTO, ECO:0007744|PDB:1HET,
FT ECO:0007744|PDB:1HLD, ECO:0007744|PDB:1JU9,
FT ECO:0007744|PDB:1LDE, ECO:0007744|PDB:1LDY,
FT ECO:0007744|PDB:1MG0, ECO:0007744|PDB:1MGO,
FT ECO:0007744|PDB:1N8K, ECO:0007744|PDB:1N92,
FT ECO:0007744|PDB:1P1R, ECO:0007744|PDB:1QLH,
FT ECO:0007744|PDB:1QLJ, ECO:0007744|PDB:1QV6,
FT ECO:0007744|PDB:1QV7, ECO:0007744|PDB:1YE3,
FT ECO:0007744|PDB:2JHG, ECO:0007744|PDB:2OHX,
FT ECO:0007744|PDB:3BTO, ECO:0007744|PDB:3OQ6,
FT ECO:0007744|PDB:4DWV, ECO:0007744|PDB:4DXH,
FT ECO:0007744|PDB:4NFH, ECO:0007744|PDB:4NFS,
FT ECO:0007744|PDB:4NG5, ECO:0007744|PDB:4XD2,
FT ECO:0007744|PDB:5ADH, ECO:0007744|PDB:6ADH,
FT ECO:0007744|PDB:7ADH, ECO:0007744|PDB:8ADH"
FT BINDING 200..205
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:15299346,
FT ECO:0007744|PDB:1ADB, ECO:0007744|PDB:1AXE,
FT ECO:0007744|PDB:1BTO, ECO:0007744|PDB:1HET,
FT ECO:0007744|PDB:1HEU, ECO:0007744|PDB:1HF3,
FT ECO:0007744|PDB:1HLD, ECO:0007744|PDB:1JU9,
FT ECO:0007744|PDB:1LDE, ECO:0007744|PDB:1LDY,
FT ECO:0007744|PDB:1MG0, ECO:0007744|PDB:1MGO,
FT ECO:0007744|PDB:1N8K, ECO:0007744|PDB:1N92,
FT ECO:0007744|PDB:1P1R, ECO:0007744|PDB:1QV6,
FT ECO:0007744|PDB:1QV7, ECO:0007744|PDB:2JHF,
FT ECO:0007744|PDB:2JHG, ECO:0007744|PDB:2OHX,
FT ECO:0007744|PDB:2OXI, ECO:0007744|PDB:3BTO,
FT ECO:0007744|PDB:3OQ6, ECO:0007744|PDB:4DWV,
FT ECO:0007744|PDB:4DXH, ECO:0007744|PDB:4NFH,
FT ECO:0007744|PDB:4XD2, ECO:0007744|PDB:6ADH"
FT BINDING 224
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:15299346,
FT ECO:0007744|PDB:1A71, ECO:0007744|PDB:1ADB,
FT ECO:0007744|PDB:1AXE, ECO:0007744|PDB:1AXG,
FT ECO:0007744|PDB:1BTO, ECO:0007744|PDB:1HET,
FT ECO:0007744|PDB:1HEU, ECO:0007744|PDB:1HF3,
FT ECO:0007744|PDB:1HLD, ECO:0007744|PDB:1JU9,
FT ECO:0007744|PDB:1LDE, ECO:0007744|PDB:1LDY,
FT ECO:0007744|PDB:1MG0, ECO:0007744|PDB:1MGO,
FT ECO:0007744|PDB:1N8K, ECO:0007744|PDB:1N92,
FT ECO:0007744|PDB:1P1R, ECO:0007744|PDB:1QLH,
FT ECO:0007744|PDB:1QV6, ECO:0007744|PDB:1QV7,
FT ECO:0007744|PDB:2JHF, ECO:0007744|PDB:2JHG,
FT ECO:0007744|PDB:2OHX, ECO:0007744|PDB:2OXI,
FT ECO:0007744|PDB:3BTO, ECO:0007744|PDB:3OQ6,
FT ECO:0007744|PDB:4DWV, ECO:0007744|PDB:4DXH,
FT ECO:0007744|PDB:4NFH, ECO:0007744|PDB:4NFS,
FT ECO:0007744|PDB:4NG5, ECO:0007744|PDB:4XD2,
FT ECO:0007744|PDB:5ADH, ECO:0007744|PDB:6ADH"
FT BINDING 229
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:15299346,
FT ECO:0007744|PDB:1A71, ECO:0007744|PDB:1ADB,
FT ECO:0007744|PDB:1AXE, ECO:0007744|PDB:1AXG,
FT ECO:0007744|PDB:1BTO, ECO:0007744|PDB:1HET,
FT ECO:0007744|PDB:1HEU, ECO:0007744|PDB:1HF3,
FT ECO:0007744|PDB:1HLD, ECO:0007744|PDB:1JU9,
FT ECO:0007744|PDB:1LDE, ECO:0007744|PDB:1MGO,
FT ECO:0007744|PDB:1N8K, ECO:0007744|PDB:1N92,
FT ECO:0007744|PDB:1QLH, ECO:0007744|PDB:2JHF,
FT ECO:0007744|PDB:2JHG, ECO:0007744|PDB:2OHX,
FT ECO:0007744|PDB:2OXI, ECO:0007744|PDB:3OQ6,
FT ECO:0007744|PDB:4DWV, ECO:0007744|PDB:4DXH,
FT ECO:0007744|PDB:4NFH, ECO:0007744|PDB:4NFS,
FT ECO:0007744|PDB:4NG5, ECO:0007744|PDB:4XD2,
FT ECO:0007744|PDB:5ADH, ECO:0007744|PDB:6ADH"
FT BINDING 293..295
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:15299346,
FT ECO:0007744|PDB:1A71, ECO:0007744|PDB:1ADB,
FT ECO:0007744|PDB:1AXE, ECO:0007744|PDB:1AXG,
FT ECO:0007744|PDB:1BTO, ECO:0007744|PDB:1HET,
FT ECO:0007744|PDB:1HEU, ECO:0007744|PDB:1HF3,
FT ECO:0007744|PDB:1HLD, ECO:0007744|PDB:1LDE,
FT ECO:0007744|PDB:1LDY, ECO:0007744|PDB:1MG0,
FT ECO:0007744|PDB:1MGO, ECO:0007744|PDB:1N8K,
FT ECO:0007744|PDB:1N92, ECO:0007744|PDB:1P1R,
FT ECO:0007744|PDB:1QLH, ECO:0007744|PDB:1QV6,
FT ECO:0007744|PDB:1QV7, ECO:0007744|PDB:2JHF,
FT ECO:0007744|PDB:2JHG, ECO:0007744|PDB:2OHX,
FT ECO:0007744|PDB:2OXI, ECO:0007744|PDB:3BTO,
FT ECO:0007744|PDB:3OQ6, ECO:0007744|PDB:4DWV,
FT ECO:0007744|PDB:4DXH, ECO:0007744|PDB:4NFH,
FT ECO:0007744|PDB:4NFS, ECO:0007744|PDB:4NG5,
FT ECO:0007744|PDB:4XD2, ECO:0007744|PDB:6ADH"
FT BINDING 293
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 320
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 370
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:15299346,
FT ECO:0007744|PDB:1A71, ECO:0007744|PDB:1ADB,
FT ECO:0007744|PDB:1AXE, ECO:0007744|PDB:1AXG,
FT ECO:0007744|PDB:1BTO, ECO:0007744|PDB:1HET,
FT ECO:0007744|PDB:1HEU, ECO:0007744|PDB:1HF3,
FT ECO:0007744|PDB:1HLD, ECO:0007744|PDB:1LDE,
FT ECO:0007744|PDB:1LDY, ECO:0007744|PDB:1MG0,
FT ECO:0007744|PDB:1MGO, ECO:0007744|PDB:1N8K,
FT ECO:0007744|PDB:1N92, ECO:0007744|PDB:1P1R,
FT ECO:0007744|PDB:1QV6, ECO:0007744|PDB:1QV7,
FT ECO:0007744|PDB:2JHF, ECO:0007744|PDB:2JHG,
FT ECO:0007744|PDB:2OHX, ECO:0007744|PDB:2OXI,
FT ECO:0007744|PDB:3BTO, ECO:0007744|PDB:3OQ6,
FT ECO:0007744|PDB:4DWV, ECO:0007744|PDB:4DXH,
FT ECO:0007744|PDB:4NFH, ECO:0007744|PDB:4NFS,
FT ECO:0007744|PDB:4NG5, ECO:0007744|PDB:4XD2,
FT ECO:0007744|PDB:6ADH"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:5466062"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:1ADG"
FT STRAND 8..15
FT /evidence="ECO:0007829|PDB:2JHF"
FT STRAND 17..20
FT /evidence="ECO:0007829|PDB:6NBB"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:2JHF"
FT STRAND 36..45
FT /evidence="ECO:0007829|PDB:2JHF"
FT HELIX 48..54
FT /evidence="ECO:0007829|PDB:2JHF"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:1MGO"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:2JHF"
FT STRAND 69..77
FT /evidence="ECO:0007829|PDB:2JHF"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:2JHF"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:4NFS"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:2JHF"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:4NFS"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:2JHF"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:6ADH"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:2JHF"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:2JHF"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:2JHF"
FT STRAND 147..154
FT /evidence="ECO:0007829|PDB:2JHF"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:2JHF"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:2JHF"
FT HELIX 167..170
FT /evidence="ECO:0007829|PDB:2JHF"
FT HELIX 171..174
FT /evidence="ECO:0007829|PDB:2JHF"
FT HELIX 176..185
FT /evidence="ECO:0007829|PDB:2JHF"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:2JHF"
FT STRAND 195..199
FT /evidence="ECO:0007829|PDB:2JHF"
FT HELIX 203..214
FT /evidence="ECO:0007829|PDB:2JHF"
FT STRAND 218..223
FT /evidence="ECO:0007829|PDB:2JHF"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:2JHF"
FT HELIX 230..235
FT /evidence="ECO:0007829|PDB:2JHF"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:2JHF"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:2JHF"
FT HELIX 251..258
FT /evidence="ECO:0007829|PDB:2JHF"
FT STRAND 263..268
FT /evidence="ECO:0007829|PDB:2JHF"
FT HELIX 273..282
FT /evidence="ECO:0007829|PDB:2JHF"
FT TURN 285..287
FT /evidence="ECO:0007829|PDB:2JHF"
FT STRAND 289..292
FT /evidence="ECO:0007829|PDB:2JHF"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:6ADH"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:2JHF"
FT HELIX 307..310
FT /evidence="ECO:0007829|PDB:2JHF"
FT STRAND 314..317
FT /evidence="ECO:0007829|PDB:2JHF"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:2JHF"
FT HELIX 325..337
FT /evidence="ECO:0007829|PDB:2JHF"
FT STRAND 338..341
FT /evidence="ECO:0007829|PDB:7ADH"
FT HELIX 344..346
FT /evidence="ECO:0007829|PDB:2JHF"
FT STRAND 347..352
FT /evidence="ECO:0007829|PDB:2JHF"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:2JHF"
FT HELIX 356..364
FT /evidence="ECO:0007829|PDB:2JHF"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:6ADH"
FT STRAND 369..374
FT /evidence="ECO:0007829|PDB:2JHF"
SQ SEQUENCE 375 AA; 39936 MW; DA701D2F6AB69C9D CRC64;
MSTAGKVIKC KAAVLWEEKK PFSIEEVEVA PPKAHEVRIK MVATGICRSD DHVVSGTLVT
PLPVIAGHEA AGIVESIGEG VTTVRPGDKV IPLFTPQCGK CRVCKHPEGN FCLKNDLSMP
RGTMQDGTSR FTCRGKPIHH FLGTSTFSQY TVVDEISVAK IDAASPLEKV CLIGCGFSTG
YGSAVKVAKV TQGSTCAVFG LGGVGLSVIM GCKAAGAARI IGVDINKDKF AKAKEVGATE
CVNPQDYKKP IQEVLTEMSN GGVDFSFEVI GRLDTMVTAL SCCQEAYGVS VIVGVPPDSQ
NLSMNPMLLL SGRTWKGAIF GGFKSKDSVP KLVADFMAKK FALDPLITHV LPFEKINEGF
DLLRSGESIR TILTF
