› 2ypi

X-ray diffraction
2.5Å resolution

CRYSTALLOGRAPHIC ANALYSIS OF THE COMPLEX BETWEEN TRIOSEPHOSPHATE ISOMERASE AND 2-PHOSPHOGLYCOLATE AT 2.5-ANGSTROMS RESOLUTION. IMPLICATIONS FOR CATALYSIS

Released:
DOI: 10.2210/pdb2ypi/pdb
PDB entry 2ypi coloured by chain, front view.
PDB entry 2ypi coloured by chain, side view.
PDB entry 2ypi coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Crystallographic analysis of the complex between triosephosphate isomerase and 2-phosphoglycolate at 2.5-A resolution: implications for catalysis.
Lolis E, Petsko GA
Biochemistry 29 6619-25 (1990)
PMID: 2204418

Function and Biology Details

Reaction catalysed: 
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-133703 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Triosephosphate isomerase Chains: A, B
Molecule details ›
Chains: A, B
Length: 247 amino acids
Theoretical weight: 26.7 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Not provided
UniProt:
  • Canonical: P00942 (Residues: 2-248; Coverage: 100%)
Gene names: TPI1, YD9609.05C, YDR050C
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
Spacegroup: P21
Unit cell:
a: 74.35Å b: 83.97Å c: 38.67Å
α: 90° β: 99.7° γ: 90°
R-values:
R R work R free
0.177 not available not available
Expression system: Not provided

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Citations

18 review citations

Enzyme catalysis: not different, just better.
Knowles JR. (1991)
17 more

32 mentions without citation

Molecular docking: a powerful approach for structure-based drug discovery.
Meng et al. (2011)
31 more