› 4p61

X-ray diffraction
1.34Å resolution

CHICKEN TRIOSEPHOSPHATE ISOMERASE WITH LOOP6 MUTATIONS, V167P AND W168E.

Released:
DOI: 10.2210/pdb4p61/pdb
PDB entry 4p61 coloured by chain, front view.
PDB entry 4p61 coloured by chain, side view.
PDB entry 4p61 coloured by chain, top view.
Source organism: Gallus gallus
Primary publication:
Enzyme architecture: the effect of replacement and deletion mutations of loop 6 on catalysis by triosephosphate isomerase.
Zhai X, Go MK, O'Donoghue AC, Amyes TL, Pegan SD, Wang Y, Loria JP, Mesecar AD, Richard JP
Biochemistry 53 3486-501 (2014)
PMID: 24825099

Function and Biology Details

Reactions catalysed: 
Glycerone phosphate = methylglyoxal + phosphate
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-133701 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Triosephosphate isomerase Chains: A, B
Molecule details ›
Chains: A, B
Length: 248 amino acids
Theoretical weight: 26.6 KDa
Source organism: Gallus gallus
Expression system: Escherichia coli
UniProt:
  • Canonical: P00940 (Residues: 1-248; Coverage: 100%)
Gene name: TPI1
Sequence domains: Triosephosphate isomerase
Structure domains: Aldolase class I

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: C2
Unit cell:
a: 79.357Å b: 56.017Å c: 105.782Å
α: 90° β: 92.83° γ: 90°
R-values:
R R work R free
0.166 0.164 0.205
Expression system: Escherichia coli

Quick links

Citations

3 review citations

A guide to the effects of a large portion of the residues of triosephosphate isomerase on catalysis, stability, druggability, and human disease.
Olivares-Illana et al. (2017)
2 more

2 mentions without citation

Reflections on the catalytic power of a TIM-barrel.
Richard et al. (2014)
1 more