› 2dc1

X-ray diffraction
1.9Å resolution

Crystal Structure Of L-Aspartate Dehydrogenase From Hyperthermophilic Archaeon Archaeoglobus fulgidus

Released:
DOI: 10.2210/pdb2dc1/pdb
PDB entry 2dc1 coloured by chain, front view.
PDB entry 2dc1 coloured by chain, side view.
PDB entry 2dc1 coloured by chain, top view.
Source organism: Archaeoglobus fulgidus
Primary publication:
Crystal structure of archaeal highly thermostable L-aspartate dehydrogenase/NAD/citrate ternary complex.
Yoneda K, Sakuraba H, Tsuge H, Katunuma N, Ohshima T
FEBS J 274 4315-25 (2007)
PMID: 17651440

Function and Biology Details

Reaction catalysed: 
L-aspartate + H(2)O + NAD(P)(+) = oxaloacetate + NH(3) + NAD(P)H
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-128024 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-aspartate dehydrogenase Chains: A, B
Molecule details ›
Chains: A, B
Length: 236 amino acids
Theoretical weight: 26.25 KDa
Source organism: Archaeoglobus fulgidus
Expression system: Escherichia coli
UniProt:
  • Canonical: O28440 (Residues: 1-236; Coverage: 100%)
Gene names: AF_1838, nadX
Sequence domains:
Structure domains:

Ligands and Environments


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

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: P21212
Unit cell:
a: 47.52Å b: 89.58Å c: 100.49Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.217 0.217 0.226
Expression system: Escherichia coli

Quick links

Citations

1 review citation

L-aspartate dehydrogenase: features and applications.
Li et al. (2012)
2 other articles

1 mention without citation

Evolution and multifarious horizontal transfer of an alternative biosynthetic pathway for the alternative polyamine sym-homospermidine.
Shaw et al. (2010)