› 1o8u

X-ray diffraction
2Å resolution

The 2 Angstrom Structure of 6-Oxo Camphor Hydrolase: New Structural Diversity in the Crotonase Superfamily

Released:
DOI: 10.2210/pdb1o8u/pdb
PDB entry 1o8u coloured by chain, front view.
PDB entry 1o8u coloured by chain, side view.
PDB entry 1o8u coloured by chain, top view.
Source organism: Rhodococcus erythropolis
Primary publication:
The 2-A crystal structure of 6-oxo camphor hydrolase. New structural diversity in the crotonase superfamily.
Whittingham JL, Turkenburg JP, Verma CS, Walsh MA, Grogan G
J Biol Chem 278 1744-50 (2003)
PMID: 12421807

Function and Biology Details

Reaction catalysed: 
Bornane-2,6-dione + H(2)O = ((1S)-4-hydroxy-2,2,3-trimethylcyclopent-3-enyl)acetate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188134 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
6-oxocamphor hydrolase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 257 amino acids
Theoretical weight: 28.51 KDa
Source organism: Rhodococcus erythropolis
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q93TU6 (Residues: 1-257; Coverage: 100%)
Gene name: camK
Sequence domains: Enoyl-CoA hydratase/isomerase
Structure domains: 2-enoyl-CoA Hydratase; Chain A, domain 1

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P21
Unit cell:
a: 78.95Å b: 130.41Å c: 81.32Å
α: 90° β: 114.16° γ: 90°
R-values:
R R work R free
0.149 0.147 0.19
Expression system: Escherichia coli BL21

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Citations

1 review citation

Emergent mechanistic diversity of enzyme-catalysed beta-diketone cleavage.
Grogan G. (2005)
5 other articles