› 1c7h

X-ray diffraction
2.5Å resolution

CRYSTAL STRUCTURE OF A MUTANT R75A IN KETOSTEROID ISOMERASE FROM PSEDOMONAS PUTIDA BIOTYPE B

Released:
DOI: 10.2210/pdb1c7h/pdb
PDB entry 1c7h coloured by chain, front view.
PDB entry 1c7h coloured by chain, side view.
PDB entry 1c7h coloured by chain, top view.
Source organism: Pseudomonas putida
Primary publication:
Roles of active site aromatic residues in catalysis by ketosteroid isomerase from Pseudomonas putida biotype B.
Kim DH, Nam GH, Jang DS, Choi G, Joo S, Kim JS, Oh BH, Choi KY
Biochemistry 38 13810-9 (1999)
PMID: 10529226

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 Chain: A
Molecule details ›
Chain: A
Length: 131 amino acids
Theoretical weight: 14.46 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: MACSCIENCE M18X
Spacegroup: C2221
Unit cell:
a: 36.374Å b: 96.062Å c: 74.437Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.172 0.172 0.271
Expression system: Escherichia coli

Quick links

Citations

11 citation in other articles

Determining the catalytic role of remote substrate binding interactions in ketosteroid isomerase.
Schwans et al. (2009)
10 more

1 mention without citation

A measure of the broad substrate specificity of enzymes based on 'duplicate' catalytic residues.
Chakraborty et al. (2012)