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5FQ9

Crystal structure of the OXA10 with 1C

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 Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 400
ChainResidue
ATHR107
AARG109
AHOH2170
AHOH2332
BALA197
BPRO198
BGLU199
BTYR200
BGLU229

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 401
ChainResidue
AALA98
AMET99
AGLU129
AILE146
AGLY148
AGLY149
AILE150
AHOH2147
AHOH2148
AHOH2333

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 402
ChainResidue
ALYS138
APHE139
ASER140
AGLU168
ASER172
ALEU178
AHOH2210
AHOH2334

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACT A 500
ChainResidue
AGLU199
AGLU227
AGLU229
AHOH2274
AHOH2292
AHOH2335
BTHR107

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 600
ChainResidue
AALA98
AHOH2056

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 400
ChainResidue
BLEU43
BLYS45
BSER50
BHOH2154
BHOH2156

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NA B 500
ChainResidue
BGLY20
BGLU171

site_idAC8
Number of Residues12
DetailsBinding site for Ligand C6S A 300 bound to SER A 67
ChainResidue
AALA66
ASER67
ASER115
AVAL117
AGLU129
AVAL130
ATHR206
AGLY207
APHE208
ASER209
AARG250
AHOH2331

site_idAC9
Number of Residues10
DetailsBinding site for Ligand C6S B 300 bound to SER B 67
ChainResidue
BALA66
BSER67
BKCX70
BSER115
BVAL117
BTHR206
BGLY207
BPHE208
BSER209
BARG250

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

243911

PDB entries from 2025-10-29

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