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6GOA

Structural basis for OXA-48 dimerization - R189A mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0005886cellular_componentplasma membrane
A0008658molecular_functionpenicillin binding
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0046677biological_processresponse to antibiotic
A0071555biological_processcell wall organization
B0005886cellular_componentplasma membrane
B0008658molecular_functionpenicillin binding
B0008800molecular_functionbeta-lactamase activity
B0016787molecular_functionhydrolase activity
B0017001biological_processantibiotic catabolic process
B0046677biological_processresponse to antibiotic
B0071555biological_processcell wall organization
C0005886cellular_componentplasma membrane
C0008658molecular_functionpenicillin binding
C0008800molecular_functionbeta-lactamase activity
C0016787molecular_functionhydrolase activity
C0017001biological_processantibiotic catabolic process
C0046677biological_processresponse to antibiotic
C0071555biological_processcell wall organization
D0005886cellular_componentplasma membrane
D0008658molecular_functionpenicillin binding
D0008800molecular_functionbeta-lactamase activity
D0016787molecular_functionhydrolase activity
D0017001biological_processantibiotic catabolic process
D0046677biological_processresponse to antibiotic
D0071555biological_processcell wall organization
E0005886cellular_componentplasma membrane
E0008658molecular_functionpenicillin binding
E0008800molecular_functionbeta-lactamase activity
E0016787molecular_functionhydrolase activity
E0017001biological_processantibiotic catabolic process
E0046677biological_processresponse to antibiotic
E0071555biological_processcell wall organization
F0005886cellular_componentplasma membrane
F0008658molecular_functionpenicillin binding
F0008800molecular_functionbeta-lactamase activity
F0016787molecular_functionhydrolase activity
F0017001biological_processantibiotic catabolic process
F0046677biological_processresponse to antibiotic
F0071555biological_processcell wall organization
G0005886cellular_componentplasma membrane
G0008658molecular_functionpenicillin binding
G0008800molecular_functionbeta-lactamase activity
G0016787molecular_functionhydrolase activity
G0017001biological_processantibiotic catabolic process
G0046677biological_processresponse to antibiotic
G0071555biological_processcell wall organization
H0005886cellular_componentplasma membrane
H0008658molecular_functionpenicillin binding
H0008800molecular_functionbeta-lactamase activity
H0016787molecular_functionhydrolase activity
H0017001biological_processantibiotic catabolic process
H0046677biological_processresponse to antibiotic
H0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue CL A 301
ChainResidue
AARG206
DARG206

site_idAC2
Number of Residues2
Detailsbinding site for residue CL B 301
ChainResidue
BTHR209
BARG250

site_idAC3
Number of Residues2
Detailsbinding site for residue CL C 301
ChainResidue
BARG206
CARG206

site_idAC4
Number of Residues1
Detailsbinding site for residue CL C 302
ChainResidue
CARG250

site_idAC5
Number of Residues2
Detailsbinding site for residue CL E 301
ChainResidue
EARG206
HARG206

site_idAC6
Number of Residues2
Detailsbinding site for residue CL G 301
ChainResidue
FARG206
GARG206

site_idAC7
Number of Residues2
Detailsbinding site for residue CL G 302
ChainResidue
GTHR209
GARG250

site_idAC8
Number of Residues2
Detailsbinding site for residue CL H 301
ChainResidue
HTHR209
HARG250

Functional Information from PROSITE/UniProt
site_idPS00337
Number of Residues11
DetailsBETA_LACTAMASE_D Beta-lactamase class-D active site. PaSTFKIPnSL
ChainResidueDetails
APRO68-LEU78

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsActive site: {"description":"Acyl-ester intermediate","evidences":[{"source":"PIRSR","id":"PIRSR602137-50","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"25406838","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26731698","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31358584","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32150407","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4WMC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5FAQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5FAS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6P97","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6P98","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6P99","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6P9C","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6V1O","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues24
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q8RLA6","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P13661","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsModified residue: {"description":"N6-carboxylysine","evidences":[{"source":"PIRSR","id":"PIRSR602137-50","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19477418","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25406838","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3HBR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4WMC","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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