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1HZO

STRUCTURE OF CLASS A CEPHALOSPORINASE FROM PROTEUS VULGARIS K1

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 Residues12
DetailsBINDING SITE FOR RESIDUE MES A 1000
ChainResidue
ASER70
AHOH432
AHOH547
AHOH664
ATYR105
ASER130
ATHR216
ALYS234
ATHR235
AGLY236
ASER237
AHOH328

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE MES B 1001
ChainResidue
BSER70
BTYR105
BSER130
BLYS234
BTHR235
BGLY236
BSER237
BHOH340
BHOH536
BHOH712

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Acyl-ester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU10101","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1btl
ChainResidueDetails
AGLU166
ALYS73
ASER130
ASER70

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1btl
ChainResidueDetails
BGLU166
BLYS73
BSER130
BSER70

239149

PDB entries from 2025-07-23

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