2hmf

X-ray diffraction
2.7Å resolution

Structure of a Threonine Sensitive Aspartokinase from Methanococcus jannaschii Complexed with Mg-ADP and Aspartate

Released:
Model geometry
Fit model/data
Primary publication:
The initial step in the archaeal aspartate biosynthetic pathway catalyzed by a monofunctional aspartokinase.
Acta Crystallogr Sect F Struct Biol Cryst Commun 62 962-6 (2006)
PMID: 17012784

Function and Biology Details

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-176511 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Probable aspartokinase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 469 amino acids
Theoretical weight: 51.02 KDa
Source organism: Methanocaldococcus jannaschii
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q57991 (Residues: 2-470; Coverage: 99%)
Gene name: MJ0571
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-ID-B
Spacegroup: P212121
Unit cell:
a: 101.741Å b: 104.508Å c: 192.92Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.243 0.241 0.276
Expression system: Escherichia coli BL21(DE3)