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1FR6

REFINED CRYSTAL STRUCTURE OF BETA-LACTAMASE FROM CITROBACTER FREUNDII INDICATES A MECHANISM FOR BETA-LACTAM HYDROLYSIS

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
Functional Information from PDB Data
site_idAC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE AZR A 362
ChainResidue
ASER64
ASER318
ATHR319
AGLY320
AASN346
AHOH427
AHOH439
AHOH500
BASP123
BASP124
BHOH450
ALEU119
AGLN120
ATYR150
AASN152
ATYR221
ALYS315
ATHR316
AGLY317

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE AZR B 362
ChainResidue
AASP123
BGLY63
BSER64
BGLN120
BTYR150
BASN152
BTYR221
BLYS315
BTHR316
BGLY317
BSER318
BASN346
BHOH456
BHOH462

Functional Information from PROSITE/UniProt
site_idPS00336
Number of Residues8
DetailsBETA_LACTAMASE_C Beta-lactamase class-C active site. FELGSVSK
ChainResidueDetails
APHE60-LYS67

218853

PDB entries from 2024-04-24

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