› 1kko

X-ray diffraction
1.33Å resolution

CRYSTAL STRUCTURE OF CITROBACTER AMALONATICUS METHYLASPARTATE AMMONIA LYASE

Released:
DOI: 10.2210/pdb1kko/pdb
PDB entry 1kko coloured by chain, front view.
PDB entry 1kko coloured by chain, side view.
PDB entry 1kko coloured by chain, top view.
Source organism: Citrobacter amalonaticus
Primary publication:
Insights into enzyme evolution revealed by the structure of methylaspartate ammonia lyase.
Levy CW, Buckley PA, Sedelnikova S, Kato Y, Asano Y, Rice DW, Baker PJ
Structure 10 105-13 (2002)
PMID: 11796115

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-130298 (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: 45.99 KDa
Source organism: Citrobacter amalonaticus
Expression system: Escherichia coli
UniProt:
  • Canonical: O66145 (Residues: 1-413; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand SO4 1 x SO4
1 modified residue:
Ligand MSE 20 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM30A
Spacegroup: C222
Unit cell:
a: 128.339Å b: 237.362Å c: 65.806Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.162 0.161 0.191
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

2 mentions without citation

Extension of the classical classification of β-turns.
de Brevern AG. (2016)
1 more