› 1nas

X-ray diffraction
2.1Å resolution

SEPIAPTERIN REDUCTASE COMPLEXED WITH N-ACETYL SEROTONIN

Released:
DOI: 10.2210/pdb1nas/pdb
PDB entry 1nas coloured by chain, front view.
PDB entry 1nas coloured by chain, side view.
PDB entry 1nas 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 OAA 1 x OAA
Ligand ASE 1 x ASE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P6522
Unit cell:
a: 116.96Å b: 116.96Å c: 105.21Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.166 0.166 0.202
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

Reduction of Neuropathic and Inflammatory Pain through Inhibition of the Tetrahydrobiopterin Pathway.
Latremoliere et al. (2015)
2 more