2vei

X-ray diffraction
1.89Å resolution

Structure-based enzyme engineering efforts with an inactive monomeric TIM variant: the importance of a single point mutation for generating an active site with suitable binding properties

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
homo trimer (preferred)
PDBe Complex ID:
PDB-CPX-138177 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Triosephosphate isomerase, glycosomal Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 238 amino acids
Theoretical weight: 25.69 KDa
Source organism: Trypanosoma brucei brucei
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P04789 (Residues: 2-250; Coverage: 95%)
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
X-ray source: ENRAF-NONIUS FR591
Spacegroup: P21
Unit cell:
a: 91.24Å b: 52.59Å c: 92.38Å
α: 90° β: 119.04° γ: 90°
R-values:
R R work R free
0.168 0.166 0.215
Expression system: Escherichia coli BL21