X-ray diffraction
2.5Å resolution

Crystal Structure of Human Sepiapterin Reductase in complex with NADP+

Source organism: Homo sapiens
Entry authors: Ugochukwu E, Kavanagh K, Ng S, Arrowsmith C, Edwards A, Sundstrom M, von Delft F, Oppermann U, Structural Genomics Consortium (SGC)

Function and Biology Details

Reaction catalysed:
L-erythro-7,8-dihydrobiopterin + NADP(+) = sepiapterin + NADPH
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Sepiapterin reductase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 282 amino acids
Theoretical weight: 30.55 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
  • Canonical: P35270 (Residues: 5-261; Coverage: 99%)
Gene name: SPR
Sequence domains: short chain dehydrogenase
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments

Cofactor: Ligand NAP 6 x NAP
2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: OTHER
Spacegroup: P21
Unit cell:
a: 55.274Å b: 95.001Å c: 162.825Å
α: 90° β: 90.57° γ: 90°
R R work R free
0.207 0.205 0.245
Expression system: Escherichia coli BL21(DE3)