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5B3R

Crystal structure of metallo-beta-lactamase IMP-18 from Pseudomonas aeruginosa

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 Residues5
Detailsbinding site for residue ZN A 2001
ChainResidue
AHIS95
AHIS97
AHIS157
AZN2002
ACIT2003

site_idAC2
Number of Residues5
Detailsbinding site for residue ZN A 2002
ChainResidue
ACIT2003
AASP99
ACYS176
AHIS215
AZN2001

site_idAC3
Number of Residues12
Detailsbinding site for residue CIT A 2003
ChainResidue
AHIS95
AHIS97
AASP99
AHIS157
ACYS176
ALYS179
AGLY184
AASN185
AHIS215
AZN2001
AZN2002
AHOH2159

site_idAC4
Number of Residues4
Detailsbinding site for residue ZN B 2001
ChainResidue
BHIS95
BHIS97
BHIS157
BCIT2003

site_idAC5
Number of Residues4
Detailsbinding site for residue ZN B 2002
ChainResidue
BASP99
BCYS176
BHIS215
BCIT2003

site_idAC6
Number of Residues14
Detailsbinding site for residue CIT B 2003
ChainResidue
BGLY45
BHIS95
BHIS97
BASP99
BHIS157
BCYS176
BLYS179
BLEU183
BGLY184
BASN185
BHIS215
BZN2001
BZN2002
BHOH2142

Functional Information from PROSITE/UniProt
site_idPS00744
Number of Residues13
DetailsBETA_LACTAMASE_B_2 Beta-lactamases class B signature 2. PekkILfGgCFVK
ChainResidueDetails
APRO167-LYS179

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PDB entries from 2024-06-12

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