› 1kcz

X-ray diffraction
1.9Å resolution

Crystal Structure of beta-methylaspartase from Clostridium tetanomorphum. Mg-complex.

Released:
DOI: 10.2210/pdb1kcz/pdb
PDB 1kcz coloured by chain and viewed from the front.
PDB 1kcz coloured by chain and viewed from the side.
PDB 1kcz coloured by chain and viewed from the top.
Source organism: Clostridium tetanomorphum
Primary publication:
The structure of 3-methylaspartase from Clostridium tetanomorphum functions via the common enolase chemical step.
Asuncion M, Blankenfeldt W, Barlow JN, Gani D, Naismith JH
J Biol Chem 277 8306-11 (2002)
PMID: 11748244

Function and Biology Details

Reaction catalysed: 
L-threo-3-methylaspartate = mesaconate + NH(3)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Methylaspartate ammonia-lyase Chains: A, B
Molecule details ›
Chains: A, B
Length: 413 amino acids
Theoretical weight: 45.64 KDa
Source organism: Clostridium tetanomorphum
Expression system: Escherichia coli
UniProt:
  • Canonical: Q05514 (Residues: 1-413; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand MG 2 x MG
Ligand EDO 2 x EDO
1 modified residue:
Ligand OCS 2 x OCS

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P212121
Unit cell:
a: 67.016Å b: 108.783Å c: 109.557Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.137 0.135 0.175
Expression system: Escherichia coli

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Citations

5 review citations

Enzymatic asymmetric synthesis of chiral amino acids.
Xue et al. (2018)
4 more

3 mentions without citation

Predicting Ca2+ -binding sites using refined carbon clusters.
Zhao et al. (2012)
2 more