1dqu

X-ray diffraction
2.8Å resolution

CRYSTAL STRUCTURE OF THE ISOCITRATE LYASE FROM ASPERGILLUS NIDULANS

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Isocitrate lyase Chain: A
Molecule details ›
Chain: A
Length: 538 amino acids
Theoretical weight: 60.4 KDa
Source organism: Aspergillus nidulans
Expression system: Aspergillus nidulans
UniProt:
  • Canonical: P28298 (Residues: 1-16, 18-538; Coverage: 100%)
Gene names: AN5634, acuD
Sequence domains: Isocitrate lyase family
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.6
Spacegroup: P42212
Unit cell:
a: 91.93Å b: 91.93Å c: 152.77Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.276 0.273 0.376
Expression system: Aspergillus nidulans