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

6T5Y

Crystal structure of AmpC from E.coli with Zidebactam (WCK 5107)

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
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue PEG A 601
ChainResidue
ATRP93
ALEU131
AHOH846

site_idAC2
Number of Residues16
Detailsbinding site for residue C8V A 602
ChainResidue
AASN289
ALYS315
ATHR316
AGLY317
AALA318
AASN346
AHOH722
AHOH738
AHOH741
AHOH826
AGLY63
ASER64
AGLN120
ATYR150
AASN152
ATYR221

site_idAC3
Number of Residues6
Detailsbinding site for residue ZN A 603
ChainResidue
AHIS13
AHIS13
AHIS13
ACL604
ACL604
ACL604

site_idAC4
Number of Residues9
Detailsbinding site for residue CL A 604
ChainResidue
AHIS13
AHIS13
AHIS13
AZN603
AZN603
AZN603
AHOH1070
AHOH1070
AHOH1070

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 Residues1
DetailsACT_SITE: Acyl-ester intermediate => ECO:0000255|PROSITE-ProRule:PRU10102, ECO:0000269|PubMed:6795623
ChainResidueDetails
ASER64

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
ATYR150

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ALYS315

219869

PDB entries from 2024-05-15

PDB statisticsPDBj update infoContact PDBjnumon