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2WGV

Crystal structure of the OXA-10 V117T mutant at pH 6.5 inhibited by a chloride ion

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 GOL A 1265
ChainResidue
ATHR107
BGLU229
BHOH2106
AARG109
AGLY110
AHOH2225
BALA197
BPRO198
BGLU199
BTYR200
BGLU227

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 1266
ChainResidue
AALA197
APRO198
AGLU199
ATYR200
AGLU227
AGLU229
AHOH2190
BTHR107
BARG109

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 1267
ChainResidue
ALYS138
ASER140
ASER172
AHOH2226

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 1268
ChainResidue
ALYS70
ATRP154
AHOH2053

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 1266
ChainResidue
BLYS70
BTRP154
BHOH2030

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 1269
ChainResidue
AALA98
AHOH2122

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 1270
ChainResidue
AARG250
AHOH2215

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 1271
ChainResidue
AARG131
ALYS152
AHOH2120

site_idAC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 B 1267
ChainResidue
BSER67
BSER115
BLYS205
BTHR206
BGLY207
BPHE208
BARG250
BHOH2124

site_idBC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE CIT A 1272
ChainResidue
AALA66
ASER67
ASER115
ALYS205
ATHR206
AGLY207
APHE208
AARG250
AHOH2099
AHOH2227
AHOH2228

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

246704

PDB entries from 2025-12-24

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