› 1kkr

X-ray diffraction
2.1Å resolution

CRYSTAL STRUCTURE OF CITROBACTER AMALONATICUS METHYLASPARTATE AMMONIA LYASE CONTAINING (2S,3S)-3-METHYLASPARTIC ACID

Released:
DOI: 10.2210/pdb1kkr/pdb
PDB entry 1kkr coloured by chain, front view.
PDB entry 1kkr coloured by chain, side view.
PDB entry 1kkr 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

2 bound ligands:
Ligand MG 2 x MG
Ligand 2AS 2 x 2AS
1 modified residue:
Ligand MSE 20 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: C222
Unit cell:
a: 129.537Å b: 238.933Å c: 66.269Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 0.177 0.223
Expression system: Escherichia coli

Quick links

Citations

6 review citations

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

7 mentions without citation

Engineering enzymes for noncanonical amino acid synthesis.
Almhjell et al. (2018)
6 more