6d43

X-ray diffraction
2.04Å resolution

CHARACTERIZATION OF HUMAN TRIOSEPHOSPHATE ISOMERASE S-NITROSYLATION

Released:
Source organism: Homo sapiens
Primary publication:
Characterization of human triosephosphate isomerase S-nitrosylation.
Nitric Oxide 77 26-34 (2018)
PMID: 29678765

Function and Biology Details

Reactions catalysed:
Glycerone phosphate = methylglyoxal + phosphate
D-glyceraldehyde 3-phosphate = glycerone phosphate
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-157973 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Triosephosphate isomerase Chain: A
Molecule details ›
Chain: A
Length: 246 amino acids
Theoretical weight: 26.43 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P60174 (Residues: 4-249; Coverage: 99%)
Gene names: TPI, TPI1
Sequence domains: Triosephosphate isomerase
Structure domains: Aldolase class I
Triosephosphate isomerase Chain: B
Molecule details ›
Chain: B
Length: 246 amino acids
Theoretical weight: 26.4 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P60174 (Residues: 4-249; Coverage: 99%)
Gene names: TPI, TPI1
Sequence domains: Triosephosphate isomerase
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: LNLS BEAMLINE W01B-MX2
Spacegroup: P212121
Unit cell:
a: 64.92Å b: 73.98Å c: 93.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.202 0.256
Expression system: Escherichia coli