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5FAQ

OXA-48 in complex with FPI-1465

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
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue CD A 301
ChainResidue
AGLU37
AHIS38
AGLU125
AGLU256
ACD304
AHOH547

site_idAC2
Number of Residues2
Detailsbinding site for residue CL A 302
ChainResidue
AARG206
BARG206

site_idAC3
Number of Residues5
Detailsbinding site for residue CD A 303
ChainResidue
AHOH555
AHOH586
BASP143
BHOH502
AASP143

site_idAC4
Number of Residues7
Detailsbinding site for residue CD A 304
ChainResidue
AHIS34
AGLU37
AGLU256
ACD301
AHOH463
AHOH547
AHOH595

site_idAC5
Number of Residues15
Detailsbinding site for residue 5VW A 305
ChainResidue
AALA69
ASER70
AASP101
AILE102
ASER118
AVAL120
ALYS208
ATHR209
AGLY210
ATYR211
AARG250
AHOH479
AHOH499
AHOH538
AHOH541

site_idAC6
Number of Residues1
Detailsbinding site for residue CO A 306
ChainResidue
AHIS140

site_idAC7
Number of Residues3
Detailsbinding site for residue CO B 301
ChainResidue
BHIS34
BGLU37
BGLU256

site_idAC8
Number of Residues6
Detailsbinding site for residue CO B 302
ChainResidue
AHIS140
AGLU147
AHOH453
AHOH480
BGLU147
BCO305

site_idAC9
Number of Residues1
Detailsbinding site for residue CO B 303
ChainResidue
BHIS140

site_idAD1
Number of Residues3
Detailsbinding site for residue CO B 304
ChainResidue
AHIS178
BHIS90
BHOH572

site_idAD2
Number of Residues6
Detailsbinding site for residue CO B 305
ChainResidue
AGLU147
AHOH453
AHOH480
BHIS140
BGLU147
BCO302

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 Residues2
DetailsACT_SITE: Acyl-ester intermediate => ECO:0000255|PIRSR:PIRSR602137-50, ECO:0000269|PubMed:25406838, ECO:0000269|PubMed:26731698, ECO:0000269|PubMed:31358584, ECO:0000269|PubMed:32150407, ECO:0007744|PDB:4WMC, ECO:0007744|PDB:5FAQ, ECO:0007744|PDB:5FAS, ECO:0007744|PDB:6P97, ECO:0007744|PDB:6P98, ECO:0007744|PDB:6P99, ECO:0007744|PDB:6P9C, ECO:0007744|PDB:6V1O
ChainResidueDetails
ASER70
BSER70

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q8RLA6
ChainResidueDetails
ASER70
ASER118
AARG250
BSER70
BSER118
BARG250

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P13661
ChainResidueDetails
ALYS73
BLYS73

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-carboxylysine => ECO:0000255|PIRSR:PIRSR602137-50, ECO:0000269|PubMed:19477418, ECO:0000269|PubMed:25406838, ECO:0007744|PDB:3HBR, ECO:0007744|PDB:4WMC
ChainResidueDetails
ALYS73
BLYS73

235183

PDB entries from 2025-04-23

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