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Ligands
Code Name Style Show Link
CAZ Acylated ceftazidime
EDO 1,2-ethanediol
Non-standard Residues
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Glycosylation
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Code : 5TW6   PDBj   RCSB PDB   PDBe
Header : HYDROLASE/ANTIBIOTIC
Title : CTX-M-14 P167S:E166A mutant with acylated ceftazidime molecule
Release Data : 2017-06-28
Compound :
mol_id molecule chains
1 Beta-lactamase A
ec: 3.5.2.6
fragment: UNP residues 29-291
mutation: E166A, P167S
Source :
mol_id organism_scientific expression_system
1 Escherichia coli  (taxid:562) Escherichia coli BL21(DE3)  (taxid:469008)
gene: blaCTX-M-14, beta-lactamase CTX-M-14, bla-CTX-M-14a, blaCTX-M-14a, blaCTX-M-14b, blaCTX-M-14c, blaCTX-M-27b, blatoho-3, blaUOE-2, CTX-M-14, AN206_26770, APT94_14605, BJJ90_27545, BK334_27290, ETN48_p0088, pCT_085, pHK01_011
Authors : Patel, M., Stojanoski, V., Sankaran, B., Prasad, B.V.V., Palzkill, T.
Keywords : CTX-M beta-lactamase ceftazidime acyl-enzyme complex, HYDROLASE-ANTIBIOTIC complex
Exp. method : X-RAY DIFFRACTION ( 1.700 Å )
Citation :

The Drug-Resistant Variant P167S Expands the Substrate Profile of CTX-M beta-Lactamases for Oxyimino-Cephalosporin Antibiotics by Enlarging the Active Site upon Acylation.

Patel, M.P.,Hu, L.,Stojanoski, V.  et al.
(2017)  Biochemistry  56 : 3443 - 3453

PubMed: 28613873
DOI: 10.1021/acs.biochem.7b00176

Chain : A
UniProt : Q9L5C7 (Q9L5C7_ECOLX)
Reaction: EC: Evidence:
Physiological Direction:
a beta-lactam + H2O = a substituted beta-amino acid 3.5.2.6 ARBA:ARBA00001526, RuleBase:RU361140
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