PDBe 4unk

X-ray diffraction
2Å resolution

Crystal structure of human triosephosphate isomerase (mutant N15D)

Released:
Source organism: Homo sapiens
Entry authors: DeLaMora-DeLaMora I, Torres-Larios A, Enriquez-Flores S, Mendez ST, Castillo-Villanueva A, Gomez-Manzo S, Lopez-Velazquez G, Marcial-Quino J, Torres-Arroyo A, Garcia-Torres I, Reyes-Vivas H, Oria-Hernandez J

Function and Biology Details

Reaction catalysed:
D-glyceraldehyde 3-phosphate = glycerone phosphate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Triosephosphate isomerase Chains: A, B
Molecule details ›
Chains: A, B
Length: 250 amino acids
Theoretical weight: 26.72 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P60174 (Residues: 39-286; Coverage: 87%)
  • Best match: P60174-4 (Residues: 1-167)
Gene names: TPI, TPI1
Sequence domains: Triosephosphate isomerase
Structure domains: Aldolase class I

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P212121
Unit cell:
a: 47.628Å b: 70.714Å c: 146.431Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.179 0.224
Expression system: Escherichia coli BL21(DE3)