Structure analysis

THE CRYSTALLOGRAPHIC STRUCTURE OF A HUMAN DIHYDROPTERIDINE REDUCTASE NADH BINARY COMPLEX EXPRESSED IN ESCHERICHIA COLI BY A CDNA CONSTRUCTED FROM ITS RAT HOMOLOGUE

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: 18689.92 Å2
Buried surface area: 5916.54 Å2
Dissociation area: 1,807.59 Å2
Dissociation energy (ΔGdiss): 26.84 kcal/mol
Dissociation entropy (TΔSdiss): 13.11 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-140649

Macromolecules

Chain: A
Length: 244 amino acids
Theoretical weight: 25.82 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P09417 (Residues: 1-244; Coverage: 100%)
Gene names: DHPR, QDPR, SDR33C1
Pfam: short chain dehydrogenase
InterPro:
CATH: NAD(P)-binding Rossmann-like Domain
SCOP: Tyrosine-dependent oxidoreductases

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