› 5c6r

X-ray diffraction
1.8Å resolution

Crystal structure of PH domain of ASAP1

Released:
DOI: 10.2210/pdb5c6r/pdb
PDB entry 5c6r coloured by chain, front view.
PDB entry 5c6r coloured by chain, side view.
PDB entry 5c6r coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Molecular Basis for Cooperative Binding of Anionic Phospholipids to the PH Domain of the Arf GAP ASAP1.
Jian X, Tang WK, Zhai P, Roy NS, Luo R, Gruschus JM, Yohe ME, Chen PW, Li Y, Byrd RA, Xia D, Randazzo PA
Structure 23 1977-88 (2015)
PMID: 26365802

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193035 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 150 amino acids
Theoretical weight: 17.25 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9QWY8 (Residues: 325-451; Coverage: 11%)
Gene names: Asap1, Ddef1, Kiaa1249, Shag1
Sequence domains: PH domain
Structure domains: Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)

Ligands and Environments

2 bound ligands:
Ligand PO4 2 x PO4
Ligand PGE 3 x PGE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: P43
Unit cell:
a: 48.12Å b: 48.12Å c: 111.333Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.211 0.208 0.26
Expression system: Escherichia coli

Quick links

Citations

7 review citations

ARF GTPases and their GEFs and GAPs: concepts and challenges.
Sztul et al. (2019)
6 more

3 mentions without citation

Allosteric properties of PH domains in Arf regulatory proteins.
Roy et al. (2016)
2 more