› 1tpu

X-ray diffraction
1.9Å resolution

S96P CHANGE IS A SECOND-SITE SUPPRESSOR FOR H95N SLUGGISH MUTANT TRIOSEPHOSPHATE ISOMERASE

Released:
DOI: 10.2210/pdb1tpu/pdb
PDB entry 1tpu coloured by chain, front view.
PDB entry 1tpu coloured by chain, side view.
PDB entry 1tpu coloured by chain, top view.
Source organism: Gallus gallus
Primary publication:
The structural basis for pseudoreversion of the H95N lesion by the secondary S96P mutation in triosephosphate isomerase.
Komives EA, Lougheed JC, Zhang Z, Sugio S, Narayana N, Xuong NH, Petsko GA, Ringe D
Biochemistry 35 15474-84 (1996)
PMID: 8952501

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: 26.52 KDa
Source organism: Gallus gallus
Expression system: Not provided
UniProt:
  • Canonical: P00940 (Residues: 2-248; Coverage: 100%)
Gene name: TPI1
Sequence domains: Triosephosphate isomerase
Structure domains: Aldolase class I

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 136.3Å b: 74.1Å c: 57.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.176 not available
Expression system: Not provided

Quick links

Citations

2 review citations

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

3 mentions without citation

Sequence-structure analysis of FAD-containing proteins.
Dym et al. (2001)
2 more