Structure analysis

Crystal structure of RCC1-Like domain 2 of ubiquitin ligase HERC2

X-ray diffraction
2.35Å resolution
Source organism: Homo sapiens
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 13423.48 Å2
Buried surface area: 538.31 Å2
Dissociation area: 143.75 Å2
Dissociation energy (ΔGdiss): -4.28 kcal/mol
Dissociation entropy (TΔSdiss): 2.83 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-131992
Assembly 2
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Multimeric state: monomeric
Accessible surface area: 13674.51 Å2
Buried surface area: 801.21 Å2
Dissociation area: 145.55 Å2
Dissociation energy (ΔGdiss): -4.61 kcal/mol
Dissociation entropy (TΔSdiss): 2.81 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-131992
Assembly 3
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Multimeric state: monomeric
Accessible surface area: 13607.39 Å2
Buried surface area: 1073.58 Å2
Dissociation area: 157.13 Å2
Dissociation energy (ΔGdiss): -3.88 kcal/mol
Dissociation entropy (TΔSdiss): 2.81 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-131992

Macromolecules

Chains: A, C, E
Length: 405 amino acids
Theoretical weight: 42.77 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O95714 (Residues: 2938-3342; Coverage: 8%)
Gene name: HERC2
Pfam: Regulator of chromosome condensation (RCC1) repeat
InterPro:

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