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4OQG

Crystal structure of TEM-1 beta-lactamase in complex with boron-based inhibitor EC25

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
C0008800molecular_functionbeta-lactamase activity
C0016787molecular_functionhydrolase activity
C0017001biological_processantibiotic catabolic process
C0030655biological_processbeta-lactam antibiotic catabolic process
C0046677biological_processresponse to antibiotic
D0008800molecular_functionbeta-lactamase activity
D0016787molecular_functionhydrolase activity
D0017001biological_processantibiotic catabolic process
D0030655biological_processbeta-lactam antibiotic catabolic process
D0046677biological_processresponse to antibiotic
E0008800molecular_functionbeta-lactamase activity
E0016787molecular_functionhydrolase activity
E0017001biological_processantibiotic catabolic process
E0030655biological_processbeta-lactam antibiotic catabolic process
E0046677biological_processresponse to antibiotic
F0008800molecular_functionbeta-lactamase activity
F0016787molecular_functionhydrolase activity
F0017001biological_processantibiotic catabolic process
F0030655biological_processbeta-lactam antibiotic catabolic process
F0046677biological_processresponse to antibiotic
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 2UL A 301
ChainResidue
AMET69
AGLY236
AALA237
AARG244
ASER70
AGLU104
ASER130
AASN132
AGLU166
AASN170
ALYS234
ASER235

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE 2UL B 301
ChainResidue
AGLU197
BMET69
BSER70
BGLU104
BTYR105
BSER130
BASN132
BGLU166
BPRO167
BLEU169
BASN170
BLYS234
BSER235
BGLY236
BALA237
BGLY238
BARG244

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN B 302
ChainResidue
BHIS96
BHIS96
BHOH407

site_idAC4
Number of Residues13
DetailsBINDING SITE FOR RESIDUE 2UL C 301
ChainResidue
CMET69
CSER70
CGLU104
CSER130
CASN132
CGLU166
CASN170
CLYS234
CSER235
CGLY236
CALA237
CGLY238
CARG244

site_idAC5
Number of Residues13
DetailsBINDING SITE FOR RESIDUE 2UL D 301
ChainResidue
DMET69
DSER70
DGLU104
DTYR105
DSER130
DASN132
DGLU166
DASN170
DSER235
DGLY236
DALA237
DGLU240
DARG244

site_idAC6
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 2UL F 301
ChainResidue
FMET69
FSER70
FSER130
FASN132
FGLU166
FASN170
FVAL216
FLYS234
FSER235
FGLY236
FALA237
FARG244

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

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PDB entries from 2026-02-25

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