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6S0H

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

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 301
ChainResidue
AHIS77
AHIS79
AHIS139
AKQ8310

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN A 302
ChainResidue
AASP81
ACYS158
AHIS197
AKQ8310

site_idAC3
Number of Residues4
Detailsbinding site for residue EDO A 303
ChainResidue
AILE70
ASER93
BLYS127
AGLU69

site_idAC4
Number of Residues5
Detailsbinding site for residue EDO A 305
ChainResidue
ASER99
ALEU101
ATYR134
AASP142
ALEU144

site_idAC5
Number of Residues4
Detailsbinding site for residue EDO A 306
ChainResidue
ATHR42
AASP43
AGLY67
AGLU69

site_idAC6
Number of Residues5
Detailsbinding site for residue EDO A 308
ChainResidue
AGLU10
AHIS34
ASER198
AGLU199
ALYS200

site_idAC7
Number of Residues1
Detailsbinding site for residue EDO A 309
ChainResidue
AASN128

site_idAC8
Number of Residues15
Detailsbinding site for residue KQ8 A 310
ChainResidue
ATRP28
AVAL30
ATHR32
APHE51
AHIS77
AHIS79
AASP81
AHIS139
ACYS158
ALYS161
ALEU165
AASN167
AHIS197
AZN301
AZN302

site_idAC9
Number of Residues3
Detailsbinding site for residue EDO B 401
ChainResidue
AGLN113
BSER119
BGLU120

site_idAD1
Number of Residues4
Detailsbinding site for residue ZN B 402
ChainResidue
BHIS77
BHIS79
BHIS139
BKQ8404

site_idAD2
Number of Residues4
Detailsbinding site for residue ZN B 403
ChainResidue
BASP81
BCYS158
BHIS197
BKQ8404

site_idAD3
Number of Residues19
Detailsbinding site for residue KQ8 B 404
ChainResidue
BVAL25
BTRP28
BVAL30
BVAL31
BTHR32
BPHE51
BHIS77
BHIS79
BSER80
BASP81
BHIS139
BCYS158
BLYS161
BLEU165
BGLY166
BASN167
BHIS197
BZN402
BZN403

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 site: {"evidences":[{"source":"PubMed","id":"32205343","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2020","submissionDatabase":"PDB data bank","title":"Structure of IMP-13 metallo-beta-lactamase complexed with citrate anion.","authors":["Zak K.M.","Zhou R.X.","Softley C.A.","Bostock M.J.","Sattler M.","Popowicz G.M."]}},{"source":"PDB","id":"6R73","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6R79","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6RZR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6RZS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6S0H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6YI4","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P52699","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"32205343","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

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