PDBe 3jue

X-ray diffraction
2.3Å resolution

Crystal Structure of ArfGAP and ANK repeat domain of ACAP1

Released:
Source organism: Homo sapiens
Primary publication:
Mechanistic insights into regulated cargo binding by ACAP1.
J. Biol. Chem. (2012)
PMID: 22645133

Function and Biology Details

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1 Chains: A, B
Molecule details ›
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
Sequence domains: Putative GTPase activating protein for Arf
Structure domains:

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: P21212
Unit cell:
a: 107.809Å b: 163.473Å c: 41.092Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.203 0.202 0.219
Expression system: Escherichia coli BL21