› 2jgq

X-ray diffraction
2.3Å resolution

Kinetics and structural properties of triosephosphate isomerase from Helicobacter pylori

Released:
DOI: 10.2210/pdb2jgq/pdb
PDB entry 2jgq coloured by chain, front view.
PDB entry 2jgq coloured by chain, side view.
PDB entry 2jgq coloured by chain, top view.
Source organism: Helicobacter pylori 26695
Primary publication:
Kinetic and structural properties of triosephosphate isomerase from Helicobacter pylori.
Chu CH, Lai YJ, Huang H, Sun YJ
Proteins 71 396-406 (2008)
PMID: 17957775

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-157390 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Triosephosphate isomerase Chains: A, B
Molecule details ›
Chains: A, B
Length: 233 amino acids
Theoretical weight: 26.61 KDa
Source organism: Helicobacter pylori 26695
Expression system: Escherichia coli
UniProt:
  • Canonical: P56076 (Residues: 2-234; Coverage: 100%)
Gene names: HP_0194, tpi, tpiA
Sequence domains: Triosephosphate isomerase
Structure domains: Aldolase class I

Ligands and Environments

2 bound ligands:
Ligand QGA 1 x QGA
Ligand PO4 2 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P21212
Unit cell:
a: 128.167Å b: 76.657Å c: 49.187Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.2 0.249
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Structural and functional aspects of the Helicobacter pylori secretome.
Zanotti et al. (2014)
1 more

4 mentions without citation

PocketMatch: a new algorithm to compare binding sites in protein structures.
Yeturu et al. (2008)
3 more