Structure analysis

Crystal structure of HRAS(G12V) - anti-RAS Fv complex

X-ray diffraction
2Å resolution
Source organism: Homo sapiens
Assembly composition:
hetero trimer (preferred)
Entry contents: 3 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
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Multimeric state: hetero trimer
Accessible surface area: 16221.9 Å2
Buried surface area: 4674.25 Å2
Dissociation area: 891.6 Å2
Dissociation energy (ΔGdiss): 7.55 kcal/mol
Dissociation entropy (TΔSdiss): 12.04 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-208342

Macromolecules

Chain: H
Length: 114 amino acids
Theoretical weight: 12.69 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
InterPro:
CATH: Immunoglobulins

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Chain: L
Length: 104 amino acids
Theoretical weight: 11.22 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
InterPro:
CATH: Immunoglobulins

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Chain: R
Length: 166 amino acids
Theoretical weight: 18.92 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P01112 (Residues: 1-166; Coverage: 88%)
Gene names: HRAS, HRAS1
Pfam: Ras family
InterPro:
CATH: P-loop containing nucleotide triphosphate hydrolases
SCOP: G proteins

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