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1OME

CRYSTAL STRUCTURE OF THE OMEGA LOOP DELETION MUTANT (RESIDUES 163-178 DELETED) OF BETA-LACTAMASE FROM STAPHYLOCOCCUS AUREUS PC1

Functional Information from GO Data
ChainGOidnamespacecontents
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0030655biological_processbeta-lactam antibiotic catabolic process
A0046677biological_processresponse to antibiotic
B0008800molecular_functionbeta-lactamase activity
B0016787molecular_functionhydrolase activity
B0017001biological_processantibiotic catabolic process
B0030655biological_processbeta-lactam antibiotic catabolic process
B0046677biological_processresponse to antibiotic
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 1
ChainResidue
BGLY236
BALA238
BARG244
BASN245

site_idCAT
Number of Residues4
DetailsACTIVE SITE. THE NUCLEOPHILIC RESIDUE IS SER 70.
ChainResidue
ASER70
ALYS73
ALYS234
AGLN237

Functional Information from PROSITE/UniProt
site_idPS00146
Number of Residues16
DetailsBETA_LACTAMASE_A Beta-lactamase class-A active site. FaYASTsKainSAILL
ChainResidueDetails
APHE66-LEU81

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Acyl-ester intermediate
ChainResidueDetails
ASER70
BSER70

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING:
ChainResidueDetails
ALYS234
BLYS234

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1btl
ChainResidueDetails
ALYS73
ASER130
ASER70

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1btl
ChainResidueDetails
BLYS73
BSER130
BSER70

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PDB entries from 2024-07-31

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