Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1VGN

Structure-based design of the irreversible inhibitors to metallo--lactamase (IMP-1)

Functional Information from GO Data
ChainGOidnamespacecontents
A0008270molecular_functionzinc ion binding
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0042597cellular_componentperiplasmic space
A0046677biological_processresponse to antibiotic
A0046872molecular_functionmetal ion binding
B0008270molecular_functionzinc ion binding
B0008800molecular_functionbeta-lactamase activity
B0016787molecular_functionhydrolase activity
B0017001biological_processantibiotic catabolic process
B0042597cellular_componentperiplasmic space
B0046677biological_processresponse to antibiotic
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 301
ChainResidue
AHIS77
AHIS79
AHIS139
AOPS1161

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 302
ChainResidue
AASP81
ACYS158
AHIS197
AOPS1161

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 303
ChainResidue
BHIS79
BHIS139
BZN304
BOPS1161
BHIS77

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 304
ChainResidue
BASP81
BCYS158
BHIS197
BZN303
BOPS1161

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE OPS A 1161
ChainResidue
AHIS79
AASP81
AHIS139
ALYS161
AASN167
AHIS197
AZN301
AZN302

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE OPS B 1161
ChainResidue
BHIS79
BASP81
BHIS139
BLYS161
BASN167
BHIS197
BZN303
BZN304

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACY A 401
ChainResidue
AGLU24
AVAL25
AGLY27
ATRP28
AGLY29

Functional Information from PROSITE/UniProt
site_idPS00743
Number of Residues20
DetailsBETA_LACTAMASE_B_1 Beta-lactamases class B signature 1. IsSHfHSDstGGiewlnsr.S
ChainResidueDetails
AILE74-SER93

site_idPS00744
Number of Residues13
DetailsBETA_LACTAMASE_B_2 Beta-lactamases class B signature 2. PerkILfGgCFIK
ChainResidueDetails
APRO149-LYS161

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:26482303
ChainResidueDetails
AHIS77
BASP81
BHIS139
BCYS158
BLYS161
BHIS197
AHIS79
AASP81
AHIS139
ACYS158
ALYS161
AHIS197
BHIS77
BHIS79

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P25910
ChainResidueDetails
AASN167
BASN167

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon