› 7az9

Hybrid

Function and Biology Details

Reaction catalysed: 
D-glyceraldehyde 3-phosphate = glycerone phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155740 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Triosephosphate isomerase Chain: A
Molecule details ›
Chain: A
Length: 251 amino acids
Theoretical weight: 27.21 KDa
Source organism: Leishmania mexicana
Expression system: Escherichia coli
UniProt:
  • Canonical: P48499 (Residues: 1-251; Coverage: 100%)
Sequence domains: Triosephosphate isomerase

Ligands and Environments

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

Experiments and Validation Details

Experimental Method: Neutron Diffraction, X-ray diffraction
X-ray source: PETRA III, EMBL c/o DESY BEAMLINE P14 (MX2), ILL BEAMLINE LADI III
Spacegroup: C2
Unit cell:
a: 98.323Å b: 52.678Å c: 58.665Å
α: 90° β: 117.86° γ: 90°
R-values:
R R work R free
0.144 0.144 0.158
Expression system: Escherichia coli

Quick links

Citations

5 citation in other articles

The impact of folding modes and deuteration on the atomic resolution structure of hen egg-white lysozyme.
Ramos et al. (2021)
4 more

1 mention without citation

Neutron structures of Leishmania mexicana triosephosphate isomerase in complex with reaction-intermediate mimics shed light on the proton-shuttling steps.
Kelpšas et al. (2021)