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5YD7

Crystal Structure OF VIM-2 Metallo-beta-lactamase

Functional Information from GO Data
ChainGOidnamespacecontents
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0046872molecular_functionmetal ion binding
B0016787molecular_functionhydrolase activity
B0017001biological_processantibiotic catabolic process
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue ZN A 301
ChainResidue
AASP118
ACYS198
AHIS240
AHOH424
AHOH471

site_idAC2
Number of Residues5
Detailsbinding site for residue ZN A 302
ChainResidue
AHOH424
AHIS114
AHIS116
AHIS179
AHOH422

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN A 303
ChainResidue
AHIS153
AHIS251
AFMT304
AFMT305

site_idAC4
Number of Residues7
Detailsbinding site for residue FMT A 304
ChainResidue
AALA132
AHIS153
AHIS251
AASN254
AZN303
AFMT305
AHOH401

site_idAC5
Number of Residues7
Detailsbinding site for residue FMT A 305
ChainResidue
AALA132
ATHR152
AHIS153
AHIS251
AZN303
AFMT304
AHOH549

site_idAC6
Number of Residues6
Detailsbinding site for residue ZN B 301
ChainResidue
BASP118
BCYS198
BHIS240
BZN302
BFMT306
BHOH427

site_idAC7
Number of Residues6
Detailsbinding site for residue ZN B 302
ChainResidue
BHIS114
BHIS116
BHIS179
BZN301
BHOH412
BHOH427

site_idAC8
Number of Residues4
Detailsbinding site for residue ZN B 303
ChainResidue
BHIS153
BHIS251
BFMT304
BFMT305

site_idAC9
Number of Residues8
Detailsbinding site for residue FMT B 304
ChainResidue
BALA132
BTHR133
BTHR152
BHIS153
BHIS251
BZN303
BFMT305
BHOH441

site_idAD1
Number of Residues7
Detailsbinding site for residue FMT B 305
ChainResidue
BALA132
BHIS153
BHIS251
BASN254
BZN303
BFMT304
BHOH401

site_idAD2
Number of Residues7
Detailsbinding site for residue FMT B 306
ChainResidue
BHIS179
BCYS198
BASN210
BHIS240
BZN301
BHOH448
BHOH522

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PDB entries from 2024-10-30

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