› 2xft

X-ray diffraction
1.8Å resolution

Structural and mechanistic studies on a cephalosporin esterase from the clavulanic acid biosynthesis pathway

Released:
DOI: 10.2210/pdb2xft/pdb
PDB entry 2xft coloured by chain, front view.
PDB entry 2xft coloured by chain, side view.
PDB entry 2xft coloured by chain, top view.
Source organism: Streptomyces clavuligerus
Primary publication:
Structural and mechanistic studies of the orf12 gene product from the clavulanic acid biosynthesis pathway.
Valegård K, Iqbal A, Kershaw NJ, Ivison D, Généreux C, Dubus A, Blikstad C, Demetriades M, Hopkinson RJ, Lloyd AJ, Roper DI, Schofield CJ, Andersson I, McDonough MA
Acta Crystallogr D Biol Crystallogr 69 1567-79 (2013)
PMID: 23897479

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-185208 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
beta-lactamase Chains: A, B
Molecule details ›
Chains: A, B
Length: 458 amino acids
Theoretical weight: 49.89 KDa
Source organism: Streptomyces clavuligerus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8KRB7 (Residues: 9-466; Coverage: 98%)
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P21
Unit cell:
a: 61.068Å b: 100.056Å c: 81.271Å
α: 90° β: 93.64° γ: 90°
R-values:
R R work R free
0.196 0.194 0.236
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

Penicillin-Binding Proteins, β-Lactamases, and β-Lactamase Inhibitors in β-Lactam-Producing Actinobacteria: Self-Resistance Mechanisms.
Martin et al. (2022)
6 other articles