Structure analysis

Crystal Structure of the human MST1-RASSF5 SARAH heterodimer

X-ray diffraction
2.281Å resolution
Source organism: Homo sapiens
Assembly composition:
hetero dimer (preferred)
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
Download    3D Visualisation
Multimeric state: hetero dimer
Accessible surface area: 6765.56 Å2
Buried surface area: 2402.46 Å2
Dissociation area: 1,201.23 Å2
Dissociation energy (ΔGdiss): 14.62 kcal/mol
Dissociation entropy (TΔSdiss): 9.96 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-171514

Macromolecules

Chain: A
Length: 51 amino acids
Theoretical weight: 6.12 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q13043 (Residues: 432-480; Coverage: 10%)
Gene names: KRS2, MST1, STK4
Pfam: C terminal SARAH domain of Mst1
InterPro:
CATH: p53-like tetramerisation domain

Search similar proteins

Chain: B
Length: 55 amino acids
Theoretical weight: 6.52 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q8WWW0 (Residues: 366-418; Coverage: 13%)
Gene names: NORE1, RAPL, RASSF5
Pfam: Novel Ras effector 1 C-terminal SARAH (Sav/Rassf/Hpo) domain
InterPro:
CATH: Single alpha-helices involved in coiled-coils or other helix-helix interfaces

Search similar proteins