› 1sep

X-ray diffraction
1.95Å resolution

MOUSE SEPIAPTERIN REDUCTASE COMPLEXED WITH NADP AND SEPIAPTERIN

Released:
DOI: 10.2210/pdb1sep/pdb
PDB entry 1sep coloured by chain, front view.
PDB entry 1sep coloured by chain, side view.
PDB entry 1sep coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
The 1.25 A crystal structure of sepiapterin reductase reveals its binding mode to pterins and brain neurotransmitters.
Auerbach G, Herrmann A, Gütlich M, Fischer M, Jacob U, Bacher A, Huber R
EMBO J 16 7219-30 (1997)
PMID: 9405351

Function and Biology Details

Reaction catalysed: 
L-erythro-7,8-dihydrobiopterin + NADP(+) = sepiapterin + NADPH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-179110 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Sepiapterin reductase Chain: A
Molecule details ›
Chain: A
Length: 261 amino acids
Theoretical weight: 27.91 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q64105 (Residues: 1-261; Coverage: 100%)
Gene name: Spr
Sequence domains: short chain dehydrogenase
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments


Cofactor: Ligand NAP 1 x NAP
1 bound ligand:
Ligand BIO 1 x BIO
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P6522
Unit cell:
a: 116.42Å b: 116.42Å c: 104.52Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.174 0.174 0.214
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Tetrahydrobiopterin biosynthesis, regeneration and functions.
Thöny et al. (2000)
8 more

5 mentions without citation

Sepiapterin reductase: Characteristics and role in diseases.
Wu et al. (2020)
4 more