Structure analysis

CRYSTAL STRUCTURE ANALYSIS OF RAC1-GDP IN COMPLEX WITH ARFAPTIN (P41)

X-ray diffraction
2.7Å resolution
Source organism: Homo sapiens
Assembly composition:
hetero trimer (preferred)
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
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Multimeric state: hetero trimer
Accessible surface area: 28055.31 Å2
Buried surface area: 6804.36 Å2
Dissociation area: 885.85 Å2
Dissociation energy (ΔGdiss): 3.12 kcal/mol
Dissociation entropy (TΔSdiss): 12.53 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-156793
Assembly 2
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Multimeric state: hetero trimer
Accessible surface area: 29205.19 Å2
Buried surface area: 5632.75 Å2
Dissociation area: 2,413.52 Å2
Dissociation energy (ΔGdiss): 19.09 kcal/mol
Dissociation entropy (TΔSdiss): 25.41 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-156793

Macromolecules

Chains: A, B
Length: 224 amino acids
Theoretical weight: 25.61 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P53365 (Residues: 118-341; Coverage: 66%)
Gene names: ARFIP2, POR1
Pfam: Arfaptin-like domain
InterPro:
CATH: Arfaptin homology (AH) domain/BAR domain
SCOP: Arfaptin, Rac-binding fragment

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Chain: D
Length: 192 amino acids
Theoretical weight: 21.48 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P63000 (Residues: 1-192; Coverage: 100%)
Gene names: MIG5, RAC1, TC25
Pfam: Ras family
InterPro:
CATH: P-loop containing nucleotide triphosphate hydrolases
SCOP: G proteins

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