4jeq

X-ray diffraction
2.3Å resolution

Different Contribution of Conserved Amino Acids to the Global Properties of Homologous Enzymes

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-138176 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Triosephosphate isomerase, glycosomal Chains: A, B, C, D, E, F, G, H, I, J, K, L
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L
Length: 250 amino acids
Theoretical weight: 26.85 KDa
Source organism: Trypanosoma cruzi
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P04789 (Residues: 1-250; Coverage: 100%)
Sequence domains: Triosephosphate isomerase
Structure domains: Aldolase class I

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: OTHER
Spacegroup: P21
Unit cell:
a: 88.087Å b: 89.782Å c: 181.718Å
α: 90° β: 101.61° γ: 90°
R-values:
R R work R free
0.21 0.207 0.261
Expression system: Escherichia coli BL21(DE3)