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3P98

The crystal structure of the extended spectrum beta-lactamase TEM-72 reveals inhibition by citrate

Functional Information from GO Data
ChainGOidnamespacecontents
A0008800molecular_functionbeta-lactamase activity
A0017001biological_processantibiotic catabolic process
A0030655biological_processbeta-lactam antibiotic catabolic process
A0046677biological_processresponse to antibiotic
B0008800molecular_functionbeta-lactamase activity
B0017001biological_processantibiotic catabolic process
B0030655biological_processbeta-lactam antibiotic catabolic process
B0046677biological_processresponse to antibiotic
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE CIT B 1
ChainResidue
BMET69
BGLY236
BALA237
BARG244
BHOH369
BSER70
BLYS73
BTYR105
BSER130
BASN132
BASN170
BLYS234
BSER235

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE CIT A 1
ChainResidue
AMET69
ASER70
ATYR105
ASER130
AASN170
ASER235
AGLY236
AALA237
AARG244

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PEG A 290
ChainResidue
AARG222
ALEU225
AHOH359
AHOH387
BALA86
BGLY87

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PEG B 290
ChainResidue
ALYS192
BARG61
BGLU64
BHOH382

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

249697

PDB entries from 2026-02-25

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