Structure analysis

Crystal Structure of Human Sepiapterin Reductase in complex with NADP+

X-ray diffraction
2.5Å resolution
Source organism: Homo sapiens
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: homo dimer
Accessible surface area: 21400 Å2
Buried surface area: 7000 Å2
Dissociation area: 1,900 Å2
Dissociation energy (ΔGdiss): 32 kcal/mol
Dissociation entropy (TΔSdiss): 13 kcal/mol
Interface energy (ΔGint): -84 kcal/mol
Symmetry number: 2
Assembly 2
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Multimeric state: homo dimer

Binding statistics and energies are not available for this assembly
Assembly 3
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Multimeric state: homo dimer

Binding statistics and energies are not available for this assembly

Macromolecules

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)
UniProt:
  • Canonical: P35270 (Residues: 5-261; Coverage: 99%)
Gene name: SPR
Pfam: short chain dehydrogenase
InterPro:
CATH: NAD(P)-binding Rossmann-like Domain
SCOP: Tyrosine-dependent oxidoreductases

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