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2HPB

Crystal structure of the OXA-10 W154A mutant at pH 9.0

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 Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 401
ChainResidue
AARG160
AHOH610

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 402
ChainResidue
AHOH404
AHOH456
AHOH575
ASER67
ASER115
ALYS205
ATHR206
AGLY207
APHE208
AARG250

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 403
ChainResidue
BSER67
BSER115
BTHR206
BGLY207
BPHE208
BARG250
BHOH432

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 B 404
ChainResidue
BARG160
BHOH455

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 405
ChainResidue
BARG131
BLYS134
BTYR135
BLYS256

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

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1m6k
ChainResidueDetails
ASER67

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1m6k
ChainResidueDetails
BSER67

244693

PDB entries from 2025-11-12

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