› 6bve

X-ray diffraction
1.78Å 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)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Triosephosphate isomerase Chains: A, B
Molecule details ›
Chains: A, B
Length: 245 amino acids
Theoretical weight: 26.47 KDa
Source organism: Synechocystis sp. PCC 6803 substr. Kazusa
Expression system: Escherichia coli
UniProt:
  • Canonical: Q59994 (Residues: 1-242; Coverage: 100%)
Gene names: slr0783, tpi, tpiA
Sequence domains: Triosephosphate isomerase
Structure domains: Aldolase class I

Ligands and Environments

2 bound ligands:
Ligand NA 2 x NA
Ligand PGA 2 x PGA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-002+
Spacegroup: P212121
Unit cell:
a: 72.88Å b: 73.099Å c: 85.175Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.156 0.154 0.19
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

Structural basis for the modulation of plant cytosolic triosephosphate isomerase activity by mimicry of redox-based modifications.
Castro-Torres et al. (2019)