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3O87

Crystal structure of AmpC beta-lactamase in complex with a sulfonamide boronic acid inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0030288cellular_componentouter membrane-bounded periplasmic space
A0042597cellular_componentperiplasmic space
A0046677biological_processresponse to antibiotic
B0008800molecular_functionbeta-lactamase activity
B0016787molecular_functionhydrolase activity
B0017001biological_processantibiotic catabolic process
B0030288cellular_componentouter membrane-bounded periplasmic space
B0042597cellular_componentperiplasmic space
B0046677biological_processresponse to antibiotic
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE BSG A 1
ChainResidue
ASER64
AHOH577
AHOH579
ATYR150
AASN152
AVAL211
ASER212
ATYR221
AALA318
AGLY320
AHOH575

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 3
ChainResidue
AHIS186
AHOH372
AHOH581
AHOH611
BLYS290

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE BSG B 2
ChainResidue
BSER64
BGLN120
BTYR150
BASN152
BVAL211
BSER212
BALA318
BGLY320
BHOH450
BHOH578
BHOH580

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Acyl-ester intermediate => ECO:0000255|PROSITE-ProRule:PRU10102, ECO:0000269|PubMed:6795623
ChainResidueDetails
ASER64
BSER64

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
ATYR150
BTYR150

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ALYS315
BLYS315

219869

PDB entries from 2024-05-15

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