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2DOO

The structure of IMP-1 complexed with the detecting reagent (DansylC4SH) by a fluorescent probe

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 501
ChainResidue
AHIS77
AHIS79
AHIS139
AC4H601

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 502
ChainResidue
AASP81
ACYS158
AHIS197
AC4H601

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 503
ChainResidue
BHIS79
BHIS139
BC4H602
BHIS77

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 504
ChainResidue
BASP81
BCYS158
BHIS197
BC4H602

site_idAC5
Number of Residues21
DetailsBINDING SITE FOR RESIDUE C4H A 601
ChainResidue
AVAL25
ATRP28
AVAL31
AHIS77
AHIS79
AASP81
AHIS139
ACYS158
ALYS161
ATYR163
AGLY164
ALEU165
AGLY166
AHIS197
AZN501
AZN502
AHOH607
AHOH663
AHOH674
BGLU211
BGLN212

site_idAC6
Number of Residues19
DetailsBINDING SITE FOR RESIDUE C4H B 602
ChainResidue
AGLU211
AGLN212
BTRP28
BVAL31
BHIS79
BASP81
BHIS139
BCYS158
BLYS161
BTYR163
BGLY164
BGLY166
BHIS197
BZN503
BZN504
BHOH637
BHOH648
BHOH658
BHOH663

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 2024-07-10

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