› 1ssg

X-ray diffraction
2.9Å resolution

Understanding protein lids: Structural analysis of active hinge mutants in triosephosphate isomerase

Released:
DOI: 10.2210/pdb1ssg/pdb
PDB entry 1ssg coloured by chain, front view.
PDB entry 1ssg coloured by chain, side view.
PDB entry 1ssg 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: 247 amino acids
Theoretical weight: 26.59 KDa
Source organism: Gallus gallus
Expression system: Escherichia coli
UniProt:
  • Canonical: P00940 (Residues: 2-248; Coverage: 100%)
Gene name: TPI1
Sequence domains: Triosephosphate isomerase
Structure domains: Aldolase class I

Ligands and Environments

3 bound ligands:
Ligand PGA 2 x PGA
Ligand SO4 4 x SO4
Ligand GOL 3 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS
Spacegroup: P41212
Unit cell:
a: 88.327Å b: 88.327Å c: 163.874Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.207 0.205 0.244
Expression system: Escherichia coli

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Citations

3 review citations

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