› 1kcz

X-ray diffraction
1.9Å resolution

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

Released:
DOI: 10.2210/pdb1kcz/pdb
PDB entry 1kcz coloured by chain, front view.
PDB entry 1kcz coloured by chain, side view.
PDB entry 1kcz coloured by chain, top view.
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)
Assembly name:
PDBe Complex ID:
PDB-CPX-170213 (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

6 review citations

Divergent evolution in the enolase superfamily: the interplay of mechanism and specificity.
Gerlt et al. (2005)
5 more

3 mentions without citation

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