› 1ylp

X-ray diffraction
1.2Å resolution

Atomic resolution structure of CTX-M-27 beta-lactamase

Released:
DOI: 10.2210/pdb1ylp/pdb
PDB entry 1ylp coloured by chain, front view.
PDB entry 1ylp coloured by chain, side view.
PDB entry 1ylp coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Atomic resolution structures of CTX-M beta-lactamases: extended spectrum activities from increased mobility and decreased stability.
Chen Y, Delmas J, Sirot J, Shoichet B, Bonnet R
J Mol Biol 348 349-62 (2005)
PMID: 15811373

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-182986 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Beta-lactamase Chain: A
Molecule details ›
Chain: A
Length: 263 amino acids
Theoretical weight: 27.98 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q840M4 (Residues: 29-291; Coverage: 100%)
Gene names: CTX-M-27, GRC73_24255, GRC73_24680, blaCTX-M-27
Sequence domains:
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC, FRU
Carbohydrate polymer
1 bound ligand:
Ligand SO4 7 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P212121
Unit cell:
a: 41.537Å b: 62.784Å c: 85.993Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.132 0.132 0.158
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

17 review citations

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

8 mentions without citation

Interferon regulatory factor 1 binding to p300 stimulates DNA-dependent acetylation of p53.
Dornan et al. (2004)
7 more