› 1ogz

X-ray diffraction
2.3Å resolution

Crystal Structure Of 5-3-Ketosteroid Isomerase Mutants P39A Complexed With Equilenin From Pseudomonas Testosteroni

Released:
DOI: 10.2210/pdb1ogz/pdb
PDB entry 1ogz coloured by chain, front view.
PDB entry 1ogz coloured by chain, side view.
PDB entry 1ogz coloured by chain, top view.
Source organism: Comamonas testosteroni
Primary publication:
The conserved cis-Pro39 residue plays a crucial role in the proper positioning of the catalytic base Asp38 in ketosteroid isomerase from Comamonas testosteroni.
Nam GH, Cha SS, Yun YS, Oh YH, Hong BH, Lee HS, Choi KY
Biochem J 375 297-305 (2003)
PMID: 12852789

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-524467 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Steroid Delta-isomerase Chain: A
Molecule details ›
Chain: A
Length: 125 amino acids
Theoretical weight: 13.4 KDa
Source organism: Comamonas testosteroni
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P00947 (Residues: 1-125; Coverage: 100%)
Gene name: ksi
Sequence domains: SnoaL-like domain
Structure domains: Nuclear Transport Factor 2; Chain: A,

Ligands and Environments

1 bound ligand:
Ligand EQU 1 x EQU
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 6B
Spacegroup: P6522
Unit cell:
a: 60.733Å b: 60.733Å c: 142.803Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.235 0.235 0.309
Expression system: Escherichia coli BL21

Quick links

Citations

7 citation in other articles

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

3 mentions without citation

A Concise Review of Biomolecule Visualization.
Li et al. (2024)
2 more