› 1vj1

X-ray diffraction
2.1Å resolution

Function and Biology Details

Reaction catalysed: 
11-alpha-hydroxy-9,15-dioxoprost-5-enoate + NAD(P)(+) = (5Z)-(13E)-11-alpha-hydroxy-9,15-dioxoprosta-5,13-dienoate + NAD(P)H
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-186567 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Prostaglandin reductase 2 Chain: A
Molecule details ›
Chain: A
Length: 363 amino acids
Theoretical weight: 39.97 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8VDQ1 (Residues: 1-351; Coverage: 100%)
Gene names: Ptgr2, Zadh1
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 9 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: P212121
Unit cell:
a: 42.386Å b: 91.805Å c: 100.565Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.18 0.216
Expression system: Escherichia coli

Quick links

Citations

7 citation in other articles

Crystal structures and catalytic mechanism of the Arabidopsis cinnamyl alcohol dehydrogenases AtCAD5 and AtCAD4.
Youn et al. (2006)
6 more

2 mentions without citation

Predicting small ligand binding sites in proteins using backbone structure.
Bordner AJ. (2008)
1 more