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

1FCO

CRYSTAL STRUCTURE OF THE E. COLI AMPC BETA-LACTAMASE COVALENTLY ACYLATED WITH THE INHIBITORY BETA-LACTAM, MOXALACTAM

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 MOX A 961
ChainResidue
ASER61
AHOH1001
AHOH1010
ALEU116
ATYR147
AASN149
ATYR218
AGLY314
AALA315
ATHR316
AGLY317

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE MOX B 961
ChainResidue
BSER61
BLYS64
BGLN117
BTYR147
BASN149
BVAL208
BALA217
BTYR218
BASN286
BLEU290
BGLY314
BALA315
BASN343
BHOH968
BHOH984
BHOH1006
BHOH1025
BHOH1028

Functional Information from PROSITE/UniProt
site_idPS00336
Number of Residues8
DetailsBETA_LACTAMASE_C Beta-lactamase class-C active site. FELGSVSK
ChainResidueDetails
APHE57-LYS64

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
ASER61
BSER61

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
ATYR147
BTYR147

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ALYS312
BLYS312

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1xx2
ChainResidueDetails
ASER61
ALYS64
AGLU269
ATYR147
ALYS312

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 1xx2
ChainResidueDetails
BSER61
BLYS64
BGLU269
BTYR147
BLYS312

219515

PDB entries from 2024-05-08

PDB statisticsPDBj update infoContact PDBjnumon