Structure analysis

Crystal Structure of ArfGAP and ANK repeat domain of ACAP1

X-ray diffraction
2.3Å resolution
Source organism: Homo sapiens
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1
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Multimeric state: monomeric
Accessible surface area: 11721.52 Å2
Buried surface area: 389.22 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-172164
Assembly 2 (preferred)
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Multimeric state: monomeric
Accessible surface area: 12112.15 Å2
Buried surface area: 190.08 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-172164

Macromolecules

Chains: A, B
Length: 368 amino acids
Theoretical weight: 39.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q15027 (Residues: 378-740; Coverage: 49%)
Gene names: ACAP1, CENTB1, KIAA0050
Pfam:
InterPro:
CATH:

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