› 1nf0

X-ray diffraction
1.6Å resolution

Triosephosphate Isomerase in Complex with DHAP

Released:
DOI: 10.2210/pdb1nf0/pdb
PDB entry 1nf0 coloured by chain, front view.
PDB entry 1nf0 coloured by chain, side view.
PDB entry 1nf0 coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Optimal alignment for enzymatic proton transfer: structure of the Michaelis complex of triosephosphate isomerase at 1.2-A resolution.
Jogl G, Rozovsky S, McDermott AE, Tong L
Proc Natl Acad Sci U S A 100 50-5 (2003)
PMID: 12509510

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: 26.65 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
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 13P 2 x 13P
1 modified residue:
Ligand FTR 2 x FTR

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE A1
Spacegroup: P212121
Unit cell:
a: 47.258Å b: 62.17Å c: 160.684Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.209 0.268
Expression system: Escherichia coli

Quick links

Citations

11 review citations

Ab initio quantum chemical and mixed quantum mechanics/molecular mechanics (QM/MM) methods for studying enzymatic catalysis.
Friesner et al. (2005)
10 more

3 mentions without citation

Optimal alignment for enzymatic proton transfer: structure of the Michaelis complex of triosephosphate isomerase at 1.2-A resolution.
Jogl et al. (2003)
2 more