Structure analysis

Crystal structure of the DH-PH-PH domain of FARP1

X-ray diffraction
4.09Å 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: 18280.66 Å2
Buried surface area: 0.0 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-195238
Assembly 2
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Multimeric state: monomeric
Accessible surface area: 19022.37 Å2
Buried surface area: 0.0 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-195238

Macromolecules

Chains: A, B
Length: 501 amino acids
Theoretical weight: 57.92 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9Y4F1 (Residues: 539-1035; Coverage: 48%)
Gene names: CDEP, FARP1, PLEKHC2
Pfam:
InterPro:

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