› 5tw6

X-ray diffraction
1.7Å resolution

CTX-M-14 P167S:E166A mutant with acylated ceftazidime molecule

Released:
DOI: 10.2210/pdb5tw6/pdb
Model geometry
Fit model/data
PDB entry 5tw6 coloured by chain, front view.
PDB entry 5tw6 coloured by chain, side view.
PDB entry 5tw6 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
The Drug-Resistant Variant P167S Expands the Substrate Profile of CTX-M β-Lactamases for Oxyimino-Cephalosporin Antibiotics by Enlarging the Active Site upon Acylation.
Patel MP, Hu L, Stojanoski V, Sankaran B, Prasad BVV, Palzkill T
Biochemistry 56 3443-3453 (2017)
PMID: 28613873

Function and Biology Details

Reaction catalysed: 
A beta-lactam + H(2)O = a substituted beta-amino acid
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192210 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase Chain: A
Molecule details ›
Chain: A
Length: 263 amino acids
Theoretical weight: 27.93 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9L5C7 (Residues: 29-291; Coverage: 100%)
Gene names: BKL28_004840, BKL28_005521, BXT93_06855, CR538_26855, CTX-M-14, E4K51_21070, EIA08_25160, ETN48_p0088, HL563_21800, HL563_23665, HLZ39_20540, HLZ39_26710, IDONEFKE_05417, NY836_21775, RCS101_P0028, RCS103_P0010, RCS30_P0082, RCS56_P0085, RCS60_P0031, RCS63_P0006, RCS65_P0008, RCS66_P0053, RCS68_P0054, SAMEA4362930_00013, SAMEA4363083_00099, SAMEA4370290_00046, beta-lactamase CTX-M-14, bla, bla CTX-M-14, bla-CTX-M-14a, blaCTX-M-14, blaCTX-M-14a, blaCTX-M-14b, blaCTX-M-14c, blaCTX-M-27b, blaUOE-2, bla_2, blatoho-3, pCT_085, pHK01_011
Sequence domains:
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

2 bound ligands:
Ligand CAZ 1 x CAZ
Ligand EDO 2 x EDO
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ALS BEAMLINE 5.0.1
Spacegroup: P3221
Unit cell:
a: 41.54Å b: 41.54Å c: 231.151Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.181 0.179 0.222
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Molecular Mechanisms, Epidemiology, and Clinical Importance of β-Lactam Resistance in Enterobacteriaceae.
De Angelis et al. (2020)
1 more

3 mentions without citation

Structural and Mechanistic Basis for Extended-Spectrum Drug-Resistance Mutations in Altering the Specificity of TEM, CTX-M, and KPC β-lactamases.
Palzkill T. (2018)
2 more