Structure analysis

Cryo-EM structure of TRIP13 in complex with ATP gamma S, p31comet, C-Mad2 and Cdc20

Electron Microscopy
4.6Å resolution
Source organism: Homo sapiens
Assembly composition:
hetero nonamer (preferred)
Entry contents: 4 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
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Multimeric state: hetero nonamer
Accessible surface area: 110223.73 Å2
Buried surface area: 36111.54 Å2
Dissociation area: 800.42 Å2
Dissociation energy (ΔGdiss): 3.72 kcal/mol
Dissociation entropy (TΔSdiss): 7.37 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-171410

Macromolecules

Chains: A, B, C, D, E, F
Length: 432 amino acids
Theoretical weight: 48.61 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q15645 (Residues: 1-432; Coverage: 100%)
Gene names: PCH2, TRIP13
Pfam: ATPase family associated with various cellular activities (AAA)
InterPro:

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Chain: P
Length: 274 amino acids
Theoretical weight: 31.09 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q15013 (Residues: 1-274; Coverage: 100%)
Gene names: CMT2, KIAA0110, MAD2L1BP
Pfam: Mad1 and Cdc20-bound-Mad2 binding
InterPro: Mad1/Cdc20-bound-Mad2 binding protein

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Chain: Q
Length: 499 amino acids
Theoretical weight: 54.8 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: Q12834 (Residues: 1-499; Coverage: 100%)
Gene name: CDC20
Pfam:
InterPro:

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Chain: Z
Length: 205 amino acids
Theoretical weight: 23.53 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: Q13257 (Residues: 1-205; Coverage: 100%)
Gene names: MAD2, MAD2L1
Pfam: HORMA domain
InterPro:

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