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1JJT

IMP-1 METALLO BETA-LACTAMASE FROM PSEUDOMONAS AERUGINOSA IN COMPLEX WITH A BIARYL SUCCINIC ACID INHIBITOR (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 Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 251
ChainResidue
AHIS77
AHIS79
AHIS139
ABDS250
AZN252

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 252
ChainResidue
AZN251
AASP81
ACYS158
AHIS197
ABDS250

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT A 260
ChainResidue
ALYS8
AHIS34
AGLU199
AZN261
AHOH1016

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 261
ChainResidue
AHIS34
AGLU199
AACT260
AHOH1016

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 251
ChainResidue
BHIS77
BHIS79
BHIS139
BBDS250
BZN252

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 252
ChainResidue
BASP81
BCYS158
BHIS197
BBDS250
BZN251

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT B 260
ChainResidue
BLYS8
BHIS34
BGLU199
BZN261

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN B 261
ChainResidue
BHIS34
BGLU199
BACT260

site_idAC9
Number of Residues15
DetailsBINDING SITE FOR RESIDUE BDS A 250
ChainResidue
AVAL25
ATRP28
APHE51
AHIS77
AHIS79
ASER80
AASP81
AHIS139
ACYS158
ALYS161
AGLY166
AASN167
AHIS197
AZN251
AZN252

site_idBC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE BDS B 250
ChainResidue
BHIS77
BHIS79
BSER80
BASP81
BHIS139
BCYS158
BLYS161
BGLY166
BASN167
BHIS197
BZN251
BZN252
BHOH1221
BHOH1238
BHOH1266
BHOH1428

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

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 2bmi
ChainResidueDetails
AASP81
AASN167

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 2bmi
ChainResidueDetails
BASP81
BASN167

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 2bmi
ChainResidueDetails
AASP81

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 2bmi
ChainResidueDetails
BASP81

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PDB entries from 2024-11-06

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