BLAN1_KLEPN
ID BLAN1_KLEPN Reviewed; 270 AA.
AC C7C422;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Metallo-beta-lactamase type 2 {ECO:0000305};
DE EC=3.5.2.6 {ECO:0000269|PubMed:19770275};
DE AltName: Full=B2 metallo-beta-lactamase {ECO:0000305};
DE AltName: Full=Beta-lactamase type II {ECO:0000303|PubMed:19770275};
DE AltName: Full=Metallo-beta-lactamase NDM-1 {ECO:0000303|PubMed:19770275};
DE AltName: Full=Metallo-beta-lactamase type II {ECO:0000303|PubMed:19770275};
DE AltName: Full=New Delhi metallo-beta-lactamase-1 {ECO:0000303|PubMed:19770275};
DE Short=NDM-1 {ECO:0000303|PubMed:19770275};
DE Flags: Precursor;
GN Name=blaNDM-1 {ECO:0000303|PubMed:19770275};
OS Klebsiella pneumoniae.
OG Plasmid pKpANDM-1.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=573;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBUNIT, AND SUBSTRATE
RP SPECIFICITY.
RC STRAIN=KP-05-506;
RX PubMed=19770275; DOI=10.1128/aac.00774-09;
RA Yong D., Toleman M.A., Giske C.G., Cho H.S., Sundman K., Lee K.,
RA Walsh T.R.;
RT "Characterization of a new metallo-beta-lactamase gene, bla(NDM-1), and a
RT novel erythromycin esterase gene carried on a unique genetic structure in
RT Klebsiella pneumoniae sequence type 14 from India.";
RL Antimicrob. Agents Chemother. 53:5046-5054(2009).
RN [2]
RP EPIDEMIOLOGY.
RX PubMed=20705517; DOI=10.1016/s1473-3099(10)70143-2;
RA Kumarasamy K.K., Toleman M.A., Walsh T.R., Bagaria J., Butt F.,
RA Balakrishnan R., Chaudhary U., Doumith M., Giske C.G., Irfan S.,
RA Krishnan P., Kumar A.V., Maharjan S., Mushtaq S., Noorie T., Paterson D.L.,
RA Pearson A., Perry C., Pike R., Rao B., Ray U., Sarma J.B., Sharma M.,
RA Sheridan E., Thirunarayan M.A., Turton J., Upadhyay S., Warner M.,
RA Welfare W., Livermore D.M., Woodford N.;
RT "Emergence of a new antibiotic resistance mechanism in India, Pakistan, and
RT the UK: a molecular, biological, and epidemiological study.";
RL Lancet Infect. Dis. 10:597-602(2010).
RN [3]
RP EPIDEMIOLOGY.
RX PubMed=20577157;
RA Limbago B., Kallen A.;
RT "Detection of Enterobacteriaceae isolates carrying metallo-beta-lactamase
RT -United States, 2010.";
RL MMWR Morb. Mortal. Wkly. Rep. 59:750-750(2010).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.16 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS
RP AND ZINC IONS, COFACTOR, AND SUBUNIT.
RX PubMed=22713171; DOI=10.1021/ja303579d;
RA King D.T., Worrall L.J., Gruninger R., Strynadka N.C.;
RT "New Delhi metallo-beta-lactamase: structural insights into beta-lactam
RT recognition and inhibition.";
RL J. Am. Chem. Soc. 134:11362-11365(2012).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 29-270 IN COMPLEX WITH ZINC IONS,
RP ACTIVITY REGULATION, COFACTOR, AND SUBUNIT.
RX PubMed=25815530; DOI=10.1021/jm501844d;
RA Klingler F.M., Wichelhaus T.A., Frank D., Cuesta-Bernal J., El-Delik J.,
RA Muller H.F., Sjuts H., Gottig S., Koenigs A., Pos K.M., Pogoryelov D.,
RA Proschak E.;
RT "Approved drugs containing thiols as inhibitors of metallo-beta-lactamases:
RT strategy to combat multidrug-resistant bacteria.";
RL J. Med. Chem. 58:3626-3630(2015).
CC -!- FUNCTION: Confers resistance to the different beta-lactams antibiotics
CC (penicillin, cephalosporin and carbapenem) via the hydrolysis of the
CC beta-lactam ring. Does not confer resistance to the polymixin colistin
CC or the fluoroquinolone ciprofloxacin. {ECO:0000269|PubMed:19770275}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-lactam + H2O = a substituted beta-amino acid;
CC Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627,
CC ChEBI:CHEBI:140347; EC=3.5.2.6;
CC Evidence={ECO:0000269|PubMed:19770275};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:22713171, ECO:0000269|PubMed:25815530};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:22713171,
CC ECO:0000269|PubMed:25815530};
CC -!- ACTIVITY REGULATION: Inhibits by captopril, thiorphan, dimercaprol and
CC tiopronin (PubMed:25815530). This enzyme is not susceptible to
CC inactivation by the beta-lactamase-blocking agents clavulanic acid
CC (PubMed:19770275). {ECO:0000269|PubMed:19770275,
CC ECO:0000269|PubMed:25815530}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8 uM for cefuroxime {ECO:0000269|PubMed:19770275};
CC KM=10 uM for cefotaxime {ECO:0000269|PubMed:19770275};
CC KM=10 uM for cephalothin {ECO:0000269|PubMed:19770275};
CC KM=12 uM for piperacillin {ECO:0000269|PubMed:19770275};
CC KM=16 uM for penicillin G {ECO:0000269|PubMed:19770275};
CC KM=22 uM for ampicillin {ECO:0000269|PubMed:19770275};
CC KM=49 uM for cefoxitin {ECO:0000269|PubMed:19770275};
CC KM=49 uM for meropenem {ECO:0000269|PubMed:19770275};
CC KM=77 uM for cefepime {ECO:0000269|PubMed:19770275};
CC KM=94 uM for imipenem {ECO:0000269|PubMed:19770275};
CC KM=181 uM for ceftazidime {ECO:0000269|PubMed:19770275};
CC Note=No activity detected against the monobactam aztreonam.
CC {ECO:0000269|PubMed:19770275};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:19770275,
CC ECO:0000269|PubMed:22713171, ECO:0000269|PubMed:25815530}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC -!- MISCELLANEOUS: Enterobacteriaceae carrying this gene (identified by
CC PCR) have been isolated in Sweden, India, Pakistan, Bangladesh,
CC England, Scotland, Northern Ireland, Australia and the USA. The
CC organisms they were identified in were K.pneumoniae, Enterobacter
CC cloacae, E.coli, Proteus spp, Citrobacter freundii, Morganella
CC morganii, Providencia spp and Klebsille oxytoca. In India most isolates
CC were from community-acquired infections rather than hospital-acquired
CC infections, indicating the gene is widespread in the environment.
CC {ECO:0000269|PubMed:20577157, ECO:0000269|PubMed:20705517}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. Class-B
CC beta-lactamase family. {ECO:0000305}.
CC -!- CAUTION: Transfer of a plasmid encoding this gene has been detected
CC between bacteria within a patient (between K.pneumoniae and E.coli).
CC Additionally the gene may be encoded within a transposon.
CC {ECO:0000305}.
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DR EMBL; FN396876; CAZ39946.1; -; Genomic_DNA.
DR RefSeq; WP_004201164.1; NZ_WWEY01000004.1.
DR RefSeq; YP_005352173.1; NC_016980.1.
DR RefSeq; YP_006958736.1; NC_019153.1.
DR RefSeq; YP_006959150.1; NC_019158.1.
DR RefSeq; YP_006959255.1; NC_019162.1.
DR RefSeq; YP_006959318.1; NC_019163.1.
DR RefSeq; YP_007195502.1; NC_019889.1.
DR RefSeq; YP_007641427.1; NC_020811.1.
DR RefSeq; YP_007936899.1; NC_021180.1.
DR RefSeq; YP_008719663.1; NC_022609.1.
DR RefSeq; YP_009023060.1; NC_023908.1.
DR RefSeq; YP_009071638.1; NC_025184.1.
DR PDB; 3PG4; X-ray; 2.00 A; A=49-270.
DR PDB; 3RKJ; X-ray; 2.00 A; A/B=39-270.
DR PDB; 3RKK; X-ray; 2.35 A; A/B=39-270.
DR PDB; 3SBL; X-ray; 2.31 A; A=39-270.
DR PDB; 3SFP; X-ray; 2.27 A; A/B/C/D=39-270.
DR PDB; 3SPU; X-ray; 2.10 A; A/B/C/D/E=27-270.
DR PDB; 3SRX; X-ray; 2.50 A; A/B=37-270.
DR PDB; 3ZR9; X-ray; 1.91 A; A=42-270.
DR PDB; 4EXS; X-ray; 2.40 A; A/B=1-270.
DR PDB; 4EXY; X-ray; 1.47 A; A/B=1-270.
DR PDB; 4EY2; X-ray; 1.17 A; A/B=1-270.
DR PDB; 4EYB; X-ray; 1.16 A; A/B=1-270.
DR PDB; 4EYF; X-ray; 1.80 A; A/B=1-270.
DR PDB; 4EYL; X-ray; 1.90 A; A/B=1-270.
DR PDB; 4GYQ; X-ray; 1.35 A; A/B/C/D=31-270.
DR PDB; 4GYU; X-ray; 1.80 A; A=31-270.
DR PDB; 4H0D; X-ray; 1.50 A; A/B=31-270.
DR PDB; 4HKY; X-ray; 2.00 A; A/B=31-270.
DR PDB; 4HL1; X-ray; 1.50 A; A/B=31-270.
DR PDB; 4HL2; X-ray; 1.05 A; A/B=31-270.
DR PDB; 4RAM; X-ray; 1.50 A; A/B=31-270.
DR PDB; 4RAW; X-ray; 1.30 A; A/B=31-270.
DR PDB; 4RBS; X-ray; 2.40 A; A/B=31-270.
DR PDB; 4RL0; X-ray; 1.30 A; A/B=29-270.
DR PDB; 4RL2; X-ray; 2.01 A; A/B=29-270.
DR PDB; 4RM5; X-ray; 2.10 A; A/B/C/D=29-270.
DR PDB; 4U4L; X-ray; 1.90 A; A/B/C/D=27-270.
DR PDB; 5A5Z; X-ray; 2.60 A; A/C=29-270.
DR PDB; 5JQJ; X-ray; 1.67 A; A=29-270.
DR PDB; 5K4M; X-ray; 1.98 A; A=29-270.
DR PDB; 5N0H; X-ray; 1.90 A; A/B=29-270.
DR PDB; 5N0I; X-ray; 1.47 A; A/B=29-270.
DR PDB; 5NBK; X-ray; 2.60 A; A/C=29-270.
DR PDB; 5O2E; X-ray; 1.30 A; A/B=29-270.
DR PDB; 5O2F; X-ray; 2.01 A; A/B=29-270.
DR PDB; 5WIG; X-ray; 1.40 A; A/B=42-270.
DR PDB; 5XP6; X-ray; 0.95 A; A=29-270.
DR PDB; 5XP9; X-ray; 1.55 A; A=29-270.
DR PDB; 5ZGE; X-ray; 1.00 A; A/B=29-270.
DR PDB; 5ZGF; X-ray; 1.20 A; A=29-270.
DR PDB; 5ZGI; X-ray; 0.98 A; A=29-270.
DR PDB; 5ZGP; X-ray; 1.15 A; A/B=29-270.
DR PDB; 5ZGQ; X-ray; 1.50 A; A/B=29-270.
DR PDB; 5ZGR; X-ray; 1.15 A; A/B=29-270.
DR PDB; 5ZGT; X-ray; 1.20 A; A/B=29-270.
DR PDB; 5ZGU; X-ray; 1.55 A; A/B=29-270.
DR PDB; 5ZGV; X-ray; 1.15 A; A/B=29-270.
DR PDB; 5ZGW; X-ray; 0.95 A; A=29-270.
DR PDB; 5ZGX; X-ray; 0.95 A; A=29-270.
DR PDB; 5ZGY; X-ray; 0.95 A; A=29-270.
DR PDB; 5ZGZ; X-ray; 0.95 A; A=29-270.
DR PDB; 5ZH1; X-ray; 1.05 A; A/B=29-270.
DR PDB; 5ZIO; X-ray; 0.98 A; A=29-270.
DR PDB; 5ZJ1; X-ray; 0.96 A; A=29-270.
DR PDB; 5ZJ2; X-ray; 1.10 A; A=29-270.
DR PDB; 5ZJ7; X-ray; 0.96 A; A=29-270.
DR PDB; 5ZJ8; X-ray; 0.96 A; A=29-270.
DR PDB; 5ZJC; X-ray; 0.96 A; A=29-270.
DR PDB; 6C6I; X-ray; 1.65 A; A/B=39-63, A/B=75-270.
DR PDB; 6CAC; X-ray; 1.79 A; A/B/C/D=39-270.
DR PDB; 6D1A; X-ray; 1.25 A; A=42-270.
DR PDB; 6D1B; X-ray; 1.25 A; A=42-270.
DR PDB; 6D1C; X-ray; 1.25 A; A=42-270.
DR PDB; 6D1D; X-ray; 1.40 A; A=42-270.
DR PDB; 6D1E; X-ray; 1.15 A; A=42-270.
DR PDB; 6D1F; X-ray; 1.15 A; A=42-270.
DR PDB; 6D1G; X-ray; 1.15 A; A=42-270.
DR PDB; 6D1H; X-ray; 1.25 A; A=42-270.
DR PDB; 6D1I; X-ray; 1.10 A; A=42-270.
DR PDB; 6D1J; X-ray; 1.15 A; A=42-270.
DR PDB; 6D1K; X-ray; 1.20 A; A=42-270.
DR PDB; 6EFJ; X-ray; 1.65 A; A=42-270.
DR PDB; 6EX7; X-ray; 1.95 A; A/B=31-270.
DR PDB; 6IBS; X-ray; 1.37 A; A/B=27-270.
DR PDB; 6IBV; X-ray; 1.40 A; A/B=27-270.
DR PDB; 6JKB; X-ray; 2.44 A; A/B=28-270.
DR PDB; 6LHE; X-ray; 1.21 A; A/B=29-270.
DR PDB; 6LIP; X-ray; 0.98 A; A=29-270.
DR PDB; 6LIZ; X-ray; 1.05 A; A=29-270.
DR PDB; 6LJ0; X-ray; 1.20 A; A=29-270.
DR PDB; 6LJ1; X-ray; 1.15 A; A=29-270.
DR PDB; 6LJ2; X-ray; 1.35 A; A=29-270.
DR PDB; 6LJ4; X-ray; 1.15 A; A=29-270.
DR PDB; 6LJ5; X-ray; 1.26 A; A=29-270.
DR PDB; 6LJ6; X-ray; 1.27 A; A=29-270.
DR PDB; 6LJ7; X-ray; 1.16 A; A=29-270.
DR PDB; 6LJ8; X-ray; 1.40 A; A=29-270.
DR PDB; 6MDU; X-ray; 1.15 A; A=42-270.
DR PDB; 6MGY; X-ray; 1.60 A; A/B/C/D=31-270.
DR PDB; 6MGZ; X-ray; 1.65 A; A/B=31-270.
DR PDB; 6NY7; X-ray; 1.40 A; A=42-270.
DR PDB; 6O3R; X-ray; 1.30 A; A=42-270.
DR PDB; 6Q2Y; X-ray; 1.00 A; A/B=27-270.
DR PDB; 6Q30; X-ray; 1.50 A; A/B=27-270.
DR PDB; 6RMF; X-ray; 1.51 A; A/B=29-270.
DR PDB; 6TWT; X-ray; 0.95 A; A/B=29-270.
DR PDB; 6V1M; X-ray; 1.05 A; A=42-270.
DR PDB; 6ZYP; X-ray; 1.40 A; A/B=29-270.
DR PDB; 6ZYQ; X-ray; 1.70 A; A/B=29-270.
DR PDBsum; 3PG4; -.
DR PDBsum; 3RKJ; -.
DR PDBsum; 3RKK; -.
DR PDBsum; 3SBL; -.
DR PDBsum; 3SFP; -.
DR PDBsum; 3SPU; -.
DR PDBsum; 3SRX; -.
DR PDBsum; 3ZR9; -.
DR PDBsum; 4EXS; -.
DR PDBsum; 4EXY; -.
DR PDBsum; 4EY2; -.
DR PDBsum; 4EYB; -.
DR PDBsum; 4EYF; -.
DR PDBsum; 4EYL; -.
DR PDBsum; 4GYQ; -.
DR PDBsum; 4GYU; -.
DR PDBsum; 4H0D; -.
DR PDBsum; 4HKY; -.
DR PDBsum; 4HL1; -.
DR PDBsum; 4HL2; -.
DR PDBsum; 4RAM; -.
DR PDBsum; 4RAW; -.
DR PDBsum; 4RBS; -.
DR PDBsum; 4RL0; -.
DR PDBsum; 4RL2; -.
DR PDBsum; 4RM5; -.
DR PDBsum; 4U4L; -.
DR PDBsum; 5A5Z; -.
DR PDBsum; 5JQJ; -.
DR PDBsum; 5K4M; -.
DR PDBsum; 5N0H; -.
DR PDBsum; 5N0I; -.
DR PDBsum; 5NBK; -.
DR PDBsum; 5O2E; -.
DR PDBsum; 5O2F; -.
DR PDBsum; 5WIG; -.
DR PDBsum; 5XP6; -.
DR PDBsum; 5XP9; -.
DR PDBsum; 5ZGE; -.
DR PDBsum; 5ZGF; -.
DR PDBsum; 5ZGI; -.
DR PDBsum; 5ZGP; -.
DR PDBsum; 5ZGQ; -.
DR PDBsum; 5ZGR; -.
DR PDBsum; 5ZGT; -.
DR PDBsum; 5ZGU; -.
DR PDBsum; 5ZGV; -.
DR PDBsum; 5ZGW; -.
DR PDBsum; 5ZGX; -.
DR PDBsum; 5ZGY; -.
DR PDBsum; 5ZGZ; -.
DR PDBsum; 5ZH1; -.
DR PDBsum; 5ZIO; -.
DR PDBsum; 5ZJ1; -.
DR PDBsum; 5ZJ2; -.
DR PDBsum; 5ZJ7; -.
DR PDBsum; 5ZJ8; -.
DR PDBsum; 5ZJC; -.
DR PDBsum; 6C6I; -.
DR PDBsum; 6CAC; -.
DR PDBsum; 6D1A; -.
DR PDBsum; 6D1B; -.
DR PDBsum; 6D1C; -.
DR PDBsum; 6D1D; -.
DR PDBsum; 6D1E; -.
DR PDBsum; 6D1F; -.
DR PDBsum; 6D1G; -.
DR PDBsum; 6D1H; -.
DR PDBsum; 6D1I; -.
DR PDBsum; 6D1J; -.
DR PDBsum; 6D1K; -.
DR PDBsum; 6EFJ; -.
DR PDBsum; 6EX7; -.
DR PDBsum; 6IBS; -.
DR PDBsum; 6IBV; -.
DR PDBsum; 6JKB; -.
DR PDBsum; 6LHE; -.
DR PDBsum; 6LIP; -.
DR PDBsum; 6LIZ; -.
DR PDBsum; 6LJ0; -.
DR PDBsum; 6LJ1; -.
DR PDBsum; 6LJ2; -.
DR PDBsum; 6LJ4; -.
DR PDBsum; 6LJ5; -.
DR PDBsum; 6LJ6; -.
DR PDBsum; 6LJ7; -.
DR PDBsum; 6LJ8; -.
DR PDBsum; 6MDU; -.
DR PDBsum; 6MGY; -.
DR PDBsum; 6MGZ; -.
DR PDBsum; 6NY7; -.
DR PDBsum; 6O3R; -.
DR PDBsum; 6Q2Y; -.
DR PDBsum; 6Q30; -.
DR PDBsum; 6RMF; -.
DR PDBsum; 6TWT; -.
DR PDBsum; 6V1M; -.
DR PDBsum; 6ZYP; -.
DR PDBsum; 6ZYQ; -.
DR AlphaFoldDB; C7C422; -.
DR SMR; C7C422; -.
DR BindingDB; C7C422; -.
DR ChEMBL; CHEMBL1667695; -.
DR DrugBank; DB04272; Citric acid.
DR GeneID; 61419528; -.
DR KEGG; ag:CAZ39946; -.
DR BRENDA; 3.5.2.6; 2814.
DR SABIO-RK; C7C422; -.
DR EvolutionaryTrace; C7C422; -.
DR PRO; PR:C7C422; -.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0008800; F:beta-lactamase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0017001; P:antibiotic catabolic process; IDA:UniProtKB.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR Pfam; PF00753; Lactamase_B; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; Hydrolase; Metal-binding; Periplasm;
KW Plasmid; Signal; Zinc.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..270
FT /note="Metallo-beta-lactamase type 2"
FT /id="PRO_0000400316"
FT BINDING 120
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:22713171,
FT ECO:0000269|PubMed:25815530"
FT BINDING 122
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:22713171,
FT ECO:0000269|PubMed:25815530"
FT BINDING 124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:22713171,
FT ECO:0000269|PubMed:25815530"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:22713171,
FT ECO:0000269|PubMed:25815530"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:22713171,
FT ECO:0000269|PubMed:25815530"
FT BINDING 211
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22713171"
FT BINDING 220
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22713171"
FT BINDING 250
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:22713171,
FT ECO:0000269|PubMed:25815530"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:5ZGE"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:5XP6"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:5XP6"
FT STRAND 58..67
FT /evidence="ECO:0007829|PDB:5XP6"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:5XP6"
FT STRAND 71..82
FT /evidence="ECO:0007829|PDB:5XP6"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:5XP6"
FT HELIX 95..108
FT /evidence="ECO:0007829|PDB:5XP6"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:5XP6"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:5XP6"
FT HELIX 123..126
FT /evidence="ECO:0007829|PDB:5XP6"
FT HELIX 129..134
FT /evidence="ECO:0007829|PDB:5XP6"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:5XP6"
FT HELIX 143..148
FT /evidence="ECO:0007829|PDB:5XP6"
FT TURN 149..153
FT /evidence="ECO:0007829|PDB:5XP6"
FT STRAND 158..161
FT /evidence="ECO:0007829|PDB:5XP6"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:5XP6"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:5XP6"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:5XP6"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:5XP6"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:5XP6"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:5XP6"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:5XP6"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:3RKK"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:5XP6"
FT HELIX 229..239
FT /evidence="ECO:0007829|PDB:5XP6"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:5XP6"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:5XP6"
FT HELIX 257..267
FT /evidence="ECO:0007829|PDB:5XP6"
SQ SEQUENCE 270 AA; 28499 MW; 1B6009120B945F14 CRC64;
MELPNIMHPV AKLSTALAAA LMLSGCMPGE IRPTIGQQME TGDQRFGDLV FRQLAPNVWQ
HTSYLDMPGF GAVASNGLIV RDGGRVLVVD TAWTDDQTAQ ILNWIKQEIN LPVALAVVTH
AHQDKMGGMD ALHAAGIATY ANALSNQLAP QEGMVAAQHS LTFAANGWVE PATAPNFGPL
KVFYPGPGHT SDNITVGIDG TDIAFGGCLI KDSKAKSLGN LGDADTEHYA ASARAFGAAF
PKASMIVMSH SAPDSRAAIT HTARMADKLR
