PDBe 3eoo

X-ray diffraction
2.9Å resolution

2.9A crystal structure of methyl-isocitrate lyase from Burkholderia pseudomallei

Released:
Entry author: Seattle Structural Genomics Center for Infectious Disease (SSGCID)

Function and Biology Details

Reaction catalysed:
(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = pyruvate + succinate. 
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Methylisocitrate lyase Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P
Length: 298 amino acids
Theoretical weight: 32.01 KDa
Source organism: Burkholderia pseudomallei 1655
Expression system: Escherichia coli
Structure domains: Phosphoenolpyruvate-binding domains

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: P212121
Unit cell:
a: 163.807Å b: 172.404Å c: 179.277Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.24 0.237 0.299
Expression system: Escherichia coli