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6R73

Structure of IMP-13 metallo-beta-lactamase complexed with hydrolysed meropenem

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 Residues15
Detailsbinding site for residue LMP A 301
ChainResidue
ATRP28
AASN167
AHIS197
AZN302
AZN303
AHOH440
BTRP28
AHIS77
AHIS79
AASP81
AHIS139
ACYS158
ALYS161
AGLY164
AGLY166

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN A 302
ChainResidue
AHIS77
AHIS79
AHIS139
ALMP301

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN A 303
ChainResidue
AASP81
ACYS158
AHIS197
ALMP301

site_idAC4
Number of Residues4
Detailsbinding site for residue ZN B 302
ChainResidue
BHIS77
BHIS79
BHIS139
BLMP301

site_idAC5
Number of Residues4
Detailsbinding site for residue ZN B 303
ChainResidue
BASP81
BCYS158
BHIS197
BLMP301

site_idAC6
Number of Residues20
Detailsbinding site for Di-peptide LMP B 301 and LYS B 161
ChainResidue
ATRP28
BTRP28
BHIS79
BSER80
BASP81
BHIS139
BCYS158
BPHE159
BILE160
BPRO162
BHIS163
BGLY164
BLEU165
BGLY166
BASN167
BHIS197
BTHR209
BGLN212
BZN302
BZN303

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

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:32205343, ECO:0000269|Ref.11, ECO:0007744|PDB:6R73, ECO:0007744|PDB:6R79, ECO:0007744|PDB:6RZR, ECO:0007744|PDB:6RZS, ECO:0007744|PDB:6S0H, ECO:0007744|PDB:6YI4
ChainResidueDetails
AHIS77
BHIS139
BCYS158
BHIS197
AHIS79
AASP81
AHIS139
ACYS158
AHIS197
BHIS77
BHIS79
BASP81

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P52699
ChainResidueDetails
ALYS161
BLYS161

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:32205343
ChainResidueDetails
AASN167
BASN167

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PDB entries from 2024-07-17

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