› 1rqd

X-ray diffraction
3Å resolution

deoxyhypusine synthase holoenzyme in its low ionic strength, high pH crystal form with the inhibitor GC7 bound in the active site

Released:
DOI: 10.2210/pdb1rqd/pdb
PDB entry 1rqd coloured by chain, front view.
PDB entry 1rqd coloured by chain, side view.
PDB entry 1rqd coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
A new crystal structure of deoxyhypusine synthase reveals the configuration of the active enzyme and of an enzyme.NAD.inhibitor ternary complex.
Umland TC, Wolff EC, Park MH, Davies DR
J Biol Chem 279 28697-705 (2004)
PMID: 15100216

Function and Biology Details

Reaction catalysed: 
(1a) spermidine + NAD(+) = dehydrospermidine + NADH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155939 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Deoxyhypusine synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 369 amino acids
Theoretical weight: 41.01 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P49366 (Residues: 1-369; Coverage: 100%)
Gene names: DHPS, DS
Sequence domains: Deoxyhypusine synthase
Structure domains: Deoxyhypusine synthase

Ligands and Environments


Cofactor: Ligand NAD 2 x NAD
1 bound ligand:
Ligand GC7 2 x GC7
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X9B
Spacegroup: P3221
Unit cell:
a: 104.78Å b: 104.78Å c: 159.25Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.197 0.196 0.232
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

10 review citations

The post-translational synthesis of a polyamine-derived amino acid, hypusine, in the eukaryotic translation initiation factor 5A (eIF5A).
Park MH. (2006)
9 more

11 mentions without citation

Alteration of oligomeric state and domain architecture is essential for functional transformation between transferase and hydrolase with the same scaffold.
Koike et al. (2009)
10 more