› 2dt9

X-ray diffraction
2.15Å resolution

Crystal structure of the regulatory subunit of aspartate kinase from Thermus flavus

Released:
DOI: 10.2210/pdb2dt9/pdb
PDB entry 2dt9 coloured by chain, front view.
PDB entry 2dt9 coloured by chain, side view.
PDB entry 2dt9 coloured by chain, top view.
Source organism: Thermus thermophilus
Primary publication:
Crystal structures of the regulatory subunit of Thr-sensitive aspartate kinase from Thermus thermophilus.
Yoshida A, Tomita T, Kono H, Fushinobu S, Kuzuyama T, Nishiyama M
FEBS J 276 3124-36 (2009)
PMID: 19490113

Function and Biology Details

Reaction catalysed: 
ATP + L-aspartate = ADP + 4-phospho-L-aspartate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158262 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aspartokinase Chains: A, B
Molecule details ›
Chains: A, B
Length: 167 amino acids
Theoretical weight: 17.74 KDa
Source organism: Thermus thermophilus
Expression system: Escherichia coli
UniProt:
  • Canonical: P61489 (Residues: 245-405; Coverage: 40%)
Gene names: ask, askAB
Sequence domains:
Structure domains: Alpha-Beta Plaits

Ligands and Environments

2 bound ligands:
Ligand ACT 2 x ACT
Ligand THR 2 x THR
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: P4332
Unit cell:
a: 141.773Å b: 141.773Å c: 141.773Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.197 0.236
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Allosteric ACTion: the varied ACT domains regulating enzymes of amino-acid metabolism.
Lang et al. (2014)
8 other articles

4 mentions without citation

Cohesion group approach for evolutionary analysis of aspartokinase, an enzyme that feeds a branched network of many biochemical pathways.
Lo et al. (2009)
3 more