5e9f

X-ray diffraction
2.8Å resolution

Structural insights of isocitrate lyases from Magnaporthe oryzae

Released:

Function and Biology Details

Reactions catalysed:
Isocitrate = succinate + glyoxylate
(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = pyruvate + succinate
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-143551 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Isocitrate lyase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 560 amino acids
Theoretical weight: 62.64 KDa
Source organism: Pyricularia oryzae 70-15
Expression system: Escherichia coli
UniProt:
  • Canonical: P0CT06 (Residues: 1-547; Coverage: 100%)
Gene names: ICL1, MGG_04895
Sequence domains: Isocitrate lyase family

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-1A
Spacegroup: P212121
Unit cell:
a: 121.583Å b: 135.314Å c: 158.88Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.186 0.226
Expression system: Escherichia coli