Structure analysis

Crystal structure of the ternary complex between the human RhoA, its inhibitor and the DH/PH domain of human ARHGEF11

X-ray diffraction
2.3Å resolution
Source organism: Homo sapiens
Assembly composition:
hetero dimer (preferred)
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1
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Multimeric state: hetero dimer
Accessible surface area: 25221.85 Å2
Buried surface area: 3604.65 Å2
Dissociation area: 1,609.94 Å2
Dissociation energy (ΔGdiss): 0.24 kcal/mol
Dissociation entropy (TΔSdiss): 13.11 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-127285
Assembly 2 (preferred)
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Multimeric state: hetero dimer
Accessible surface area: 25619.05 Å2
Buried surface area: 3185.62 Å2
Dissociation area: 1,473.83 Å2
Dissociation energy (ΔGdiss): 6.85 kcal/mol
Dissociation entropy (TΔSdiss): 13.08 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-127285

Macromolecules

Chains: A, E
Length: 369 amino acids
Theoretical weight: 42.91 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O15085 (Residues: 714-1081; Coverage: 24%)
Gene names: ARHGEF11, KIAA0380
Pfam:
InterPro:
CATH:

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Chains: B, F
Length: 181 amino acids
Theoretical weight: 20.47 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P61586 (Residues: 1-181; Coverage: 94%)
Gene names: ARH12, ARHA, RHO12, RHOA
Pfam: Ras family
InterPro:
CATH: P-loop containing nucleotide triphosphate hydrolases

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