› 1h2h

X-ray diffraction
2.6Å resolution

Crystal structure of TM1643

Released:
DOI: 10.2210/pdb1h2h/pdb
PDB entry 1h2h coloured by chain, front view.
PDB entry 1h2h coloured by chain, side view.
PDB entry 1h2h coloured by chain, top view.
Source organism: Thermotoga maritima
Primary publication:
Aspartate dehydrogenase, a novel enzyme identified from structural and functional studies of TM1643.
Yang Z, Savchenko A, Yakunin A, Zhang R, Edwards A, Arrowsmith C, Tong L
J Biol Chem 278 8804-8 (2003)
PMID: 12496312

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 domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194850 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-aspartate dehydrogenase Chain: A
Molecule details ›
Chain: A
Length: 241 amino acids
Theoretical weight: 26.86 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9X1X6 (Residues: 1-241; Coverage: 100%)
Gene names: TM_1643, nadX
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 1 x NAD
No bound ligands
1 modified residue:
Ligand MSE 4 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: P41212
Unit cell:
a: 63.196Å b: 63.196Å c: 125.673Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.226 0.226 0.291
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Enzyme genomics: Application of general enzymatic screens to discover new enzymes.
Kuznetsova et al. (2005)
8 more

2 mentions without citation

Real-time ligand binding pocket database search using local surface descriptors.
Chikhi et al. (2010)
1 more