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2X02

CRYSTAL STRUCTURE OF THE CLASS D BETA-LACTAMASE OXA-10 AT 1.35 A RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
A0005886cellular_componentplasma membrane
A0008658molecular_functionpenicillin binding
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0042597cellular_componentperiplasmic space
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
B0042597cellular_componentperiplasmic space
B0046677biological_processresponse to antibiotic
B0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SO4 A 1266
ChainResidue
ASER67
AHOH2320
AHOH2321
ASER115
ALYS205
ATHR206
AGLY207
APHE208
AARG250
AHOH2060
AHOH2319

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PG4 A 1267
ChainResidue
ASER215
AASN216
AHOH2288
AHOH2322
AHOH2324
BGLN158
BARG160
BHOH2137

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PG4 B 1266
ChainResidue
AHIS87
AVAL89
BTYR174
BLEU175

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE DMS B 1267
ChainResidue
BTYR63
BLEU64
BSER209
BVAL219

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE DMS A 1270
ChainResidue
AHOH2324
BGLU62
BGLY142
BHOH2154

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE DMS A 1268
ChainResidue
ATYR63
ALEU64
APRO217
AHOH2053

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE DMS A 1269
ChainResidue
AASN29
APHE32
AVAL37
AASN38
AGLY39
AASN54
AASP55

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 1268
ChainResidue
BASN29
BPHE32
BVAL37
BASN38
BGLY39
BASN54
BASP55

Functional Information from PROSITE/UniProt
site_idPS00337
Number of Residues11
DetailsBETA_LACTAMASE_D Beta-lactamase class-D active site. PaSTFKIPnAI
ChainResidueDetails
APRO65-ILE75

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Acyl-ester intermediate","evidences":[{"source":"PubMed","id":"11724923","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19860471","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1K54","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WGI","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19860471","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2WGI","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"N6-carboxylysine","evidences":[{"source":"PubMed","id":"11188693","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11724923","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19860471","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1E4D","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1K4E","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1K4F","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1K54","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1K55","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1K56","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1K57","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1K6S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2RL3","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

250359

PDB entries from 2026-03-11

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