› 1fmc

X-ray diffraction
1.8Å resolution

7-ALPHA-HYDROXYSTEROID DEHYDROGENASE COMPLEX WITH NADH AND 7-OXO GLYCOCHENODEOXYCHOLIC ACID

Released:
DOI: 10.2210/pdb1fmc/pdb
PDB entry 1fmc coloured by chain, front view.
PDB entry 1fmc coloured by chain, side view.
PDB entry 1fmc coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structures of the binary and ternary complexes of 7 alpha-hydroxysteroid dehydrogenase from Escherichia coli.
Tanaka N, Nonaka T, Tanabe T, Yoshimoto T, Tsuru D, Mitsui Y
Biochemistry 35 7715-30 (1996)
PMID: 8672472

Function and Biology Details

Reaction catalysed: 
3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholanate + NAD(+) = 3-alpha,12-alpha-dihydroxy-7-oxo-5-beta-cholanate + NADH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142502 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
7alpha-hydroxysteroid dehydrogenase Chains: A, B
Molecule details ›
Chains: A, B
Length: 255 amino acids
Theoretical weight: 26.8 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AET8 (Residues: 1-255; Coverage: 100%)
Gene names: JW1611, b1619, hdhA, hsdH
Sequence domains: short chain dehydrogenase
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments


Cofactor: Ligand NAI 2 x NAI
1 bound ligand:
Ligand CHO 2 x CHO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-18B
Spacegroup: P41212
Unit cell:
a: 81.65Å b: 81.65Å c: 214.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.207 0.207 0.252
Expression system: Escherichia coli

Quick links

Citations

12 review citations

Bile salt biotransformations by human intestinal bacteria.
Ridlon et al. (2006)
11 more

13 mentions without citation

Virtual screening applications in short-chain dehydrogenase/reductase research.
Beck et al. (2017)
12 more