PDBe 1f8m

X-ray diffraction
1.8Å resolution

CRYSTAL STRUCTURE OF 3-BROMOPYRUVATE MODIFIED ISOCITRATE LYASE (ICL) FROM MYCOBACTERIUM TUBERCULOSIS

Released:

Function and Biology Details

Reaction catalysed:
Isocitrate = succinate + glyoxylate. 
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Isocitrate lyase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 429 amino acids
Theoretical weight: 47.21 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WKK7 (Residues: 2-428; Coverage: 100%)
Gene names: MTV038.11, Rv0467, icl
Sequence domains: Isocitrate lyase family
Structure domains: Phosphoenolpyruvate-binding domains

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P212121
Unit cell:
a: 74.31Å b: 129.037Å c: 166.165Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.212 0.203 0.247
Expression system: Escherichia coli