1n5d

X-ray diffraction
2.3Å resolution

CRYSTAL STRUCTURE OF PORCINE TESTICULAR CARBONYL REDUCTASE/ 20BETA-HYDROXYSTEROID DEHYDROGENASE

Released:

Function and Biology Details

Reactions catalysed:
R-CHOH-R' + NADP(+) = R-CO-R' + NADPH
(5Z,13E)-(15S)-9-alpha,11-alpha,15-trihydroxyprosta-5,13-dienoate + NADP(+) = (5Z,13E)-(15S)-11-alpha,15-dihydroxy-9-oxoprosta-5,13-dienoate + NADPH
(5Z,13E)-(15S)-9-alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADP(+) = (5Z,13E)-9-alpha-hydroxy-11,15-dioxoprosta-5,13-dienoate + NADPH
(13E)-(15S)-11-alpha,15-dihydroxy-9-oxoprost-13-enoate + NADP(+) = (13E)-11-alpha-hydroxy-9,15-dioxoprost-13-enoate + NADPH
An alcohol + NAD(P)(+) = an aldehyde + NAD(P)H
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-557704 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carbonyl reductase [NADPH] 1 Chain: A
Molecule details ›
Chain: A
Length: 288 amino acids
Theoretical weight: 31.6 KDa
Source organism: Sus scrofa
UniProt:
  • Canonical: Q28960 (Residues: 2-289; Coverage: 100%)
Gene names: CBR, CBR1, CRN
Sequence domains: short chain dehydrogenase
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments


Cofactor: Ligand NDP 1 x NDP
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P43212
Unit cell:
a: 58.53Å b: 58.53Å c: 165.64Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.194 0.251