› 4f1p

X-ray diffraction
2.3Å resolution

Crystal Structure of mutant S554D for ArfGAP and ANK repeat domain of ACAP1

Released:
DOI: 10.2210/pdb4f1p/pdb
PDB entry 4f1p coloured by chain, front view.
PDB entry 4f1p coloured by chain, side view.
PDB entry 4f1p coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Mechanistic insights into regulated cargo binding by ACAP1 protein.
Bai M, Pang X, Lou J, Zhou Q, Zhang K, Ma J, Li J, Sun F, Hsu VW
J Biol Chem 287 28675-85 (2012)
PMID: 22645133

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172164 (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: 39.19 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q15027 (Residues: 378-740; Coverage: 49%)
Gene names: ACAP1, CENTB1, KIAA0050
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand ZN 2 x ZN
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: P21212
Unit cell:
a: 107.561Å b: 163.46Å c: 41.184Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.218 0.217 0.235
Expression system: Escherichia coli

Quick links

Citations

3 review citations

To degrade or not to degrade: mechanisms and significance of endocytic recycling.
Cullen et al. (2018)
2 more

1 mention without citation

Mechanistic insights into regulated cargo binding by ACAP1 protein.
Bai et al. (2012)