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2ZC7

Crystal Structure of Class C beta-Lactamase ACT-1

Functional Information from GO Data
ChainGOidnamespacecontents
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0030288cellular_componentouter membrane-bounded periplasmic space
A0046677biological_processresponse to antibiotic
B0008800molecular_functionbeta-lactamase activity
B0016787molecular_functionhydrolase activity
B0017001biological_processantibiotic catabolic process
B0030288cellular_componentouter membrane-bounded periplasmic space
B0046677biological_processresponse to antibiotic
C0008800molecular_functionbeta-lactamase activity
C0016787molecular_functionhydrolase activity
C0017001biological_processantibiotic catabolic process
C0030288cellular_componentouter membrane-bounded periplasmic space
C0046677biological_processresponse to antibiotic
D0008800molecular_functionbeta-lactamase activity
D0016787molecular_functionhydrolase activity
D0017001biological_processantibiotic catabolic process
D0030288cellular_componentouter membrane-bounded periplasmic space
D0046677biological_processresponse to antibiotic
Functional Information from PROSITE/UniProt
site_idPS00336
Number of Residues8
DetailsBETA_LACTAMASE_C Beta-lactamase class-C active site. FELGSISK
ChainResidueDetails
APHE60-LYS67

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1xx2
ChainResidueDetails
AGLU272
ASER64
ALYS315
ATYR150
ALYS67

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 1xx2
ChainResidueDetails
BGLU272
BSER64
BLYS315
BTYR150
BLYS67

site_idCSA3
Number of Residues5
DetailsAnnotated By Reference To The Literature 1xx2
ChainResidueDetails
CGLU272
CSER64
CLYS315
CTYR150
CLYS67

site_idCSA4
Number of Residues5
DetailsAnnotated By Reference To The Literature 1xx2
ChainResidueDetails
DGLU272
DSER64
DLYS315
DTYR150
DLYS67

222036

PDB entries from 2024-07-03

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