Structure analysis

Crystallographic binding studies with an engineered monomeric variant of triosephosphate isomerase

X-ray diffraction
1.84Å resolution
Source organism: Trypanosoma brucei brucei
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 10178.59 Å2
Buried surface area: 646.36 Å2
Dissociation area: 88.31 Å2
Dissociation energy (ΔGdiss): 12.02 kcal/mol
Dissociation entropy (TΔSdiss): 0.59 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-138175
Assembly 2
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Multimeric state: monomeric
Accessible surface area: 10671.82 Å2
Buried surface area: 614.33 Å2
Dissociation area: 58.35 Å2
Dissociation energy (ΔGdiss): 7.78 kcal/mol
Dissociation entropy (TΔSdiss): 0.58 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-138175

Macromolecules

Chains: A, B
Length: 238 amino acids
Theoretical weight: 25.66 KDa
Source organism: Trypanosoma brucei brucei
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P04789 (Residues: 2-250; Coverage: 95%)
Pfam: Triosephosphate isomerase
InterPro:
CATH: Aldolase class I

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