› 4g1k

X-ray diffraction
2.35Å 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-173984 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Triosephosphate isomerase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 272 amino acids
Theoretical weight: 28.26 KDa
Source organism: Burkholderia thailandensis E264
Expression system: Escherichia coli
UniProt:
  • Canonical: Q2SZN7 (Residues: 1-251; Coverage: 100%)
Gene names: BTH_I1058, tpiA
Sequence domains: Triosephosphate isomerase
Structure domains: Aldolase class I

Ligands and Environments

3 bound ligands:
Ligand NA 4 x NA
Ligand EDO 11 x EDO
Ligand ACT 1 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.3
Spacegroup: P212121
Unit cell:
a: 79.51Å b: 94.75Å c: 170.61Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.171 0.17 0.202
Expression system: Escherichia coli

Quick links

Citations

11 review citations

Prokaryotic Heme Biosynthesis: Multiple Pathways to a Common Essential Product.
Dailey et al. (2017)
10 more

1 mention without citation

Combining functional and structural genomics to sample the essential Burkholderia structome.
Baugh et al. (2013)