1ttj

X-ray diffraction
2.4Å resolution

THREE NEW CRYSTAL STRUCTURES OF POINT MUTATION VARIANTS OF MONOTIM: CONFORMATIONAL FLEXIBILITY OF LOOP-1,LOOP-4 AND LOOP-8

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Triosephosphate isomerase, glycosomal Chain: A
Molecule details ›
Chain: A
Length: 243 amino acids
Theoretical weight: 26.02 KDa
Source organism: Trypanosoma brucei brucei
UniProt:
  • Canonical: P04789 (Residues: 1-250; Coverage: 97%)
Sequence domains: Triosephosphate isomerase
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 47.06Å b: 39.33Å c: 68.32Å
α: 90° β: 117.49° γ: 90°
R-values:
R R work R free
0.178 0.178 not available