› 1hdr

X-ray diffraction
2.5Å resolution

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

Released:
DOI: 10.2210/pdb1hdr/pdb
PDB entry 1hdr coloured by chain, front view.
PDB entry 1hdr coloured by chain, side view.
PDB entry 1hdr coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The crystallographic structure of a human dihydropteridine reductase NADH binary complex expressed in Escherichia coli by a cDNA constructed from its rat homologue.
Su Y, Varughese KI, Xuong NH, Bray TL, Roche DJ, Whiteley JM
J Biol Chem 268 26836-41 (1993)
PMID: 8262916

Function and Biology Details

Reaction catalysed: 
A 5,6,7,8-tetrahydropteridine + NAD(P)(+) = a 6,7-dihydropteridine + NAD(P)H
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-140649 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydropteridine reductase Chain: A
Molecule details ›
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
Sequence domains: short chain dehydrogenase
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments


Cofactor: Ligand NAD 1 x NAD
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2221
Unit cell:
a: 50.65Å b: 138.65Å c: 65.01Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.169 0.169 not available
Expression system: Not provided

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Citations

2 review citations

Tetrahydrobiopterin biosynthesis, regeneration and functions.
Thöny et al. (2000)
1 more

9 mentions without citation

Insights into Molecular Structure of Pterins Suitable for Biomedical Applications.
Buglak et al. (2022)
8 more