› 2dkn

X-ray diffraction
1.8Å resolution

Crystal structure of the 3-alpha-hydroxysteroid dehydrogenase from Pseudomonas sp. B-0831 complexed with NADH

Released:
DOI: 10.2210/pdb2dkn/pdb
PDB entry 2dkn coloured by chain, front view.
PDB entry 2dkn coloured by chain, side view.
PDB entry 2dkn coloured by chain, top view.
Source organism: Pseudomonas sp. B-0831
Primary publication:
Apo- and holo-structures of 3alpha-hydroxysteroid dehydrogenase from Pseudomonas sp. B-0831. Loop-helix transition induced by coenzyme binding.
Nakamura S, Oda M, Kataoka S, Ueda S, Uchiyama S, Yoshida T, Kobayashi Y, Ohkubo T
J Biol Chem 281 31876-84 (2006)
PMID: 16905772

Function and Biology Details

Reaction catalysed: 
A 3-alpha-hydroxysteroid + NAD(P)(+) = a 3-oxosteroid + NAD(P)H
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-176820 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-alpha-hydroxysteroid dehydrogenase Chains: A, B
Molecule details ›
Chains: A, B
Length: 255 amino acids
Theoretical weight: 25.92 KDa
Source organism: Pseudomonas sp. B-0831
Expression system: Escherichia coli
UniProt:
  • Canonical: Q59718 (Residues: 1-255; Coverage: 100%)
Sequence domains:
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments


Cofactor: Ligand NAI 1 x NAI
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL38B1
Spacegroup: P212121
Unit cell:
a: 62.457Å b: 82.248Å c: 86.569Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.172 0.205
Expression system: Escherichia coli

Quick links

Citations

8 citation in other articles

Crystal structure of a carbonyl reductase from Candida parapsilosis with anti-Prelog stereospecificity.
Zhang et al. (2008)
7 more

1 mention without citation

The catalytic roles of P185 and T188 and substrate-binding loop flexibility in 3α-hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni.
Hwang et al. (2013)