Structure analysis

Crystal Structure of human Rad GTPase

X-ray diffraction
1.8Å 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: 7100 Å2
Buried surface area: 700 Å2
Dissociation area: 100 Å2
Dissociation energy (ΔGdiss): 12 kcal/mol
Dissociation entropy (TΔSdiss): -1 kcal/mol
Interface energy (ΔGint): -15 kcal/mol
Symmetry number: 1
Assembly 2
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Multimeric state: monomeric

Binding statistics and energies are not available for this assembly

Macromolecules

Chains: A, B
Length: 174 amino acids
Theoretical weight: 19.05 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P55042 (Residues: 87-258; Coverage: 56%)
Gene names: RAD, RRAD
Pfam: Ras family
InterPro:
CATH: P-loop containing nucleotide triphosphate hydrolases

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