› 3gvg

X-ray diffraction
1.55Å resolution

Function and Biology Details

Reaction catalysed: 
D-glyceraldehyde 3-phosphate = glycerone phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161453 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Triosephosphate isomerase Chains: A, B
Molecule details ›
Chains: A, B
Length: 283 amino acids
Theoretical weight: 29.82 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WG43 (Residues: 2-261; Coverage: 100%)
Gene names: MTCY493.16c, Rv1438, tpi, tpiA
Sequence domains: Triosephosphate isomerase
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:
Ligand GOL 3 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: C2
Unit cell:
a: 133.12Å b: 55.76Å c: 76.42Å
α: 90° β: 104.01° γ: 90°
R-values:
R R work R free
0.145 0.143 0.169
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Pleiotropic Functions of Tumor Suppressor WWOX in Normal and Cancer Cells.
Abu-Remaileh et al. (2015)
5 more

1 mention without citation

Structural analysis on mutation residues and interfacial water molecules for human TIM disease understanding.
Li et al. (2013)