Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1KE3

X-ray crystal structure of AmpC beta-lactamase from E. coli in complex with the inhibitor 4,4'-biphenyldiboronic acid

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 Residues6
DetailsBINDING SITE FOR RESIDUE PO4 A 1
ChainResidue
AARG133
AHIS186
AHOH471
AHOH574
AHOH595
BLYS290

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE BDB A 364
ChainResidue
ATYR150
AASN152
ATYR221
AGLY317
AALA318
AHOH402
AHOH593
ASER64
AGLN120
AASP123

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE BDB B 364
ChainResidue
BSER64
BGLN120
BASP123
BTYR150
BASN152
BTYR221
BGLY317
BALA318
BHOH400
BHOH581

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:11478888, ECO:0000269|PubMed:16506777, ECO:0000269|PubMed:6795623, ECO:0000269|PubMed:9819201
ChainResidueDetails
ASER64
BSER64

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:16506777, ECO:0007744|PDB:2FFY
ChainResidueDetails
ASER64
ATYR150
AASN152
AALA318
BSER64
BTYR150
BASN152
BALA318

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

222415

PDB entries from 2024-07-10

PDB statisticsPDBj update infoContact PDBjnumon