7dsf

X-ray diffraction
1.8Å resolution

The Crystal Structure of human SPR from Biortus.

Released:
Model geometry
Fit model/data
Source organism: Homo sapiens
Entry authors: Wang F, Lv Z, Cheng W, Lin D, Meng Q, Zhang B, Huang Y

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)
Assembly name:
PDBe Complex ID:
PDB-CPX-152880 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Sepiapterin reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 278 amino acids
Theoretical weight: 30.09 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P35270 (Residues: 1-261; Coverage: 100%)
Gene name: SPR
Sequence domains: short chain dehydrogenase

Ligands and Environments


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

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: SPRING-8 BEAMLINE BL45XU
Spacegroup: P212121
Unit cell:
a: 55.893Å b: 74.56Å c: 121.176Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.194 0.218
Expression system: Escherichia coli