Structure analysis

Crystal structure of Podosopora anserina putative kinesin light chain nearly identical TPR-like repeats

X-ray diffraction
1.587Å resolution
Source organism: Podospora anserina
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: homo dimer
Accessible surface area: 19300 Å2
Buried surface area: 4100 Å2
Dissociation area: 2,000 Å2
Dissociation energy (ΔGdiss): 2 kcal/mol
Dissociation entropy (TΔSdiss): 13 kcal/mol
Interface energy (ΔGint): 1 kcal/mol
Symmetry number: 2

Macromolecules

Chain: A
Length: 229 amino acids
Theoretical weight: 25.83 KDa
Source organism: Podospora anserina
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A090CRQ5 (Residues: 705-925; Coverage: 21%)
Pfam: Tetratricopeptide repeat
InterPro:
CATH: Tetratricopeptide repeat domain

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