› 1oaa

X-ray diffraction
1.25Å resolution

MOUSE SEPIAPTERIN REDUCTASE COMPLEXED WITH NADP AND OXALOACETATE

Released:
DOI: 10.2210/pdb1oaa/pdb
PDB entry 1oaa coloured by chain, front view.
PDB entry 1oaa coloured by chain, side view.
PDB entry 1oaa 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: 259 amino acids
Theoretical weight: 27.65 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q64105 (Residues: 3-261; Coverage: 99%)
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
2 bound ligands:
Ligand SO4 2 x SO4
Ligand OAA 1 x OAA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: P6522
Unit cell:
a: 115.88Å b: 115.88Å c: 103.88Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.2 0.2 0.222
Expression system: Escherichia coli

Quick links

Citations

10 review citations

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

3 mentions without citation

A graph-theory algorithm for rapid protein side-chain prediction.
Canutescu et al. (2003)
2 more