› 1vzz

X-ray diffraction
2.3Å resolution

CRYSTAL STRUCTURE OF MUTANT ENZYME Y32F/D103L OF KETOSTEROID ISOMERASE FROM PSEUDOMONAS PUTIDA BIOTYPE B

Released:
DOI: 10.2210/pdb1vzz/pdb
PDB entry 1vzz coloured by chain, front view.
PDB entry 1vzz coloured by chain, side view.
PDB entry 1vzz coloured by chain, top view.
Source organism: Pseudomonas putida
Primary publication:
Structural double-mutant cycle analysis of a hydrogen bond network in ketosteroid isomerase from Pseudomonas putida biotype B.
Jang DS, Cha HJ, Cha SS, Hong BH, Ha NC, Lee JY, Oh BH, Lee HS, Choi KY
Biochem J 382 967-73 (2004)
PMID: 15228388

Function and Biology Details

Reaction catalysed: 
A 3-oxo-Delta(5)-steroid = a 3-oxo-Delta(4)-steroid
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139594 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Steroid Delta-isomerase Chains: A, B
Molecule details ›
Chains: A, B
Length: 131 amino acids
Theoretical weight: 14.53 KDa
Source organism: Pseudomonas putida
Expression system: Escherichia coli
UniProt:
  • Canonical: P07445 (Residues: 1-131; Coverage: 100%)
Gene name: ksi
Sequence domains: SnoaL-like domain
Structure domains: Nuclear Transport Factor 2; Chain: A,

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6B
Spacegroup: P212121
Unit cell:
a: 35.279Å b: 72.958Å c: 95.855Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.227 0.227 0.239
Expression system: Escherichia coli

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Citations

2 review citations

Membrane protein folding: how important are hydrogen bonds?
Bowie JU. (2011)
1 more