› 1ylz

X-ray diffraction
1.35Å resolution

X-ray crystallographic structure of CTX-M-14 beta-lactamase complexed with ceftazidime-like boronic acid

Released:
DOI: 10.2210/pdb1ylz/pdb
PDB entry 1ylz coloured by chain, front view.
PDB entry 1ylz coloured by chain, side view.
PDB entry 1ylz coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structure, function, and inhibition along the reaction coordinate of CTX-M beta-lactamases.
Chen Y, Shoichet B, Bonnet R
J Am Chem Soc 127 5423-34 (2005)
PMID: 15826180

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 263 amino acids
Theoretical weight: 28 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, 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, blatoho-3, pCT_085, pHK01_011
Sequence domains:
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

2 bound ligands:
Ligand PO4 3 x PO4
Ligand CB4 2 x CB4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P21
Unit cell:
a: 45.31Å b: 106.892Å c: 47.88Å
α: 90° β: 101.87° γ: 90°
R-values:
R R work R free
0.129 0.129 0.172
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

13 review citations

Three decades of beta-lactamase inhibitors.
Drawz et al. (2010)
12 more

1 mention without citation

Conserved water molecules stabilize the Omega-loop in class A beta-lactamases.
Bös et al. (2008)