PDBe 4br1

X-ray diffraction
1.9Å resolution

Protease-induced heterodimer of human triosephosphate isomerase.

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

Function and Biology Details

Reaction catalysed:
D-glyceraldehyde 3-phosphate = glycerone phosphate
Biochemical function:
Biological process:
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: 246 amino acids
Theoretical weight: 26.4 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P60174 (Residues: 41-286; Coverage: 86%)
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 22-ID
Spacegroup: P212121
Unit cell:
a: 68.301Å b: 77.317Å c: 87.311Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 0.177 0.217
Expression system: Escherichia coli BL21(DE3)