› 1sw7

X-ray diffraction
2.22Å resolution

Triosephosphate isomerase from Gallus gallus, loop 6 mutant K174N, T175S, A176S

Released:
DOI: 10.2210/pdb1sw7/pdb
PDB entry 1sw7 coloured by chain, front view.
PDB entry 1sw7 coloured by chain, side view.
PDB entry 1sw7 coloured by chain, top view.
Source organism: Gallus gallus
Primary publication:
Understanding protein lids: structural analysis of active hinge mutants in triosephosphate isomerase.
Kursula I, Salin M, Sun J, Norledge BV, Haapalainen AM, Sampson NS, Wierenga RK
Protein Eng Des Sel 17 375-82 (2004)
PMID: 15166315

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 domain:

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: 26.64 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

1 bound ligand:
Ligand PGA 2 x PGA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS
Spacegroup: P41212
Unit cell:
a: 87.218Å b: 87.218Å c: 162.942Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.195 0.236
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Triosephosphate isomerase: a highly evolved biocatalyst.
Wierenga et al. (2010)
2 more

1 mention without citation

Enzyme architecture: the effect of replacement and deletion mutations of loop 6 on catalysis by triosephosphate isomerase.
Zhai et al. (2014)