X-ray diffraction
1.8Å resolution

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


Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
ORF12 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)
  • Canonical: Q8KRB7 (Residues: 9-466; Coverage: 98%)
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P21
Unit cell:
a: 61.593Å b: 100.589Å c: 81.241Å
α: 90° β: 93.77° γ: 90°
R R work R free
0.216 0.214 0.261
Expression system: Escherichia coli BL21(DE3)