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6R78

Structure of IMP-13 metallo-beta-lactamase in apo form (loop closed)

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 Residues8
Detailsbinding site for residue GOL A 401
ChainResidue
AGLU14
AGLY15
AVAL16
ALEU39
AGLU150
ASER151
AHOH515
AHOH516

site_idAC2
Number of Residues2
Detailsbinding site for residue PEG A 402
ChainResidue
AHOH527
ATYR134

site_idAC3
Number of Residues2
Detailsbinding site for residue GOL A 403
ChainResidue
AASP6
ALEU7

site_idAC4
Number of Residues8
Detailsbinding site for residue GOL A 405
ChainResidue
ASER99
AGLU100
ALEU101
ASER119
AGLU120
ATYR134
AHOH519
AHOH523

site_idAC5
Number of Residues2
Detailsbinding site for residue BME A 406
ChainResidue
AHIS34
ALYS200

site_idAC6
Number of Residues5
Detailsbinding site for residue ZN A 407
ChainResidue
AHIS77
AHIS79
AHIS139
AZN408
AHOH562

site_idAC7
Number of Residues6
Detailsbinding site for residue ZN A 408
ChainResidue
AASP81
ACYS158
AHIS197
AZN407
AGOL411
AHOH562

site_idAC8
Number of Residues3
Detailsbinding site for residue NA A 409
ChainResidue
ATHR42
AASP43
AGLU69

site_idAC9
Number of Residues7
Detailsbinding site for residue EDO A 410
ChainResidue
ATHR49
ATHR73
AILE74
ASER75
AILE86
ATHR96
ATYR97

site_idAD1
Number of Residues5
Detailsbinding site for residue GOL A 411
ChainResidue
AHIS139
ALYS161
AASN167
AHIS197
AZN408

site_idAD2
Number of Residues5
Detailsbinding site for residue GOL B 301
ChainResidue
BSER99
BGLU100
BLEU101
BHOH411
BHOH443

site_idAD3
Number of Residues4
Detailsbinding site for residue GOL B 302
ChainResidue
BVAL25
BASN167
BHOH409
BHOH428

site_idAD4
Number of Residues2
Detailsbinding site for residue GOL B 303
ChainResidue
BPHE17
BTYR68

site_idAD5
Number of Residues3
Detailsbinding site for residue GOL B 304
ChainResidue
BGLU199
BLYS200
BHOH406

site_idAD6
Number of Residues4
Detailsbinding site for residue BME B 305
ChainResidue
BLEU39
BLEU148
BSER151
BHOH421

site_idAD7
Number of Residues6
Detailsbinding site for residue ZN B 306
ChainResidue
BASP81
BCYS158
BHIS197
BZN307
BHOH444
BHOH452

site_idAD8
Number of Residues6
Detailsbinding site for residue ZN B 307
ChainResidue
BHIS77
BHIS79
BHIS139
BZN306
BHOH409
BHOH452

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

246905

PDB entries from 2025-12-31

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