5i3j

X-ray diffraction
1.8Å resolution

Structure-Function Studies on Role of Hydrophobic Clamping of a Basic Glutamate in Catalysis by Triosephosphate Isomerase

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
Molecule details ›
Chains: A, B
Length: 250 amino acids
Theoretical weight: 26.82 KDa
Source organism: Trypanosoma brucei brucei
Expression system: Escherichia coli
UniProt:
  • Canonical: P04789 (Residues: 1-250; Coverage: 100%)
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: SSRL BEAMLINE BL7-1
Spacegroup: P1
Unit cell:
a: 40.03Å b: 44.12Å c: 71.7Å
α: 79.06° β: 77.49° γ: 63.11°
R-values:
R R work R free
0.166 0.163 0.211
Expression system: Escherichia coli