› 3rcp

X-ray diffraction
1.9Å resolution

Crystal structure of the FAPP1 pleckstrin homology domain

Released:
DOI: 10.2210/pdb3rcp/pdb
PDB entry 3rcp coloured by chain, front view.
PDB entry 3rcp coloured by chain, side view.
PDB entry 3rcp coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Molecular basis of phosphatidylinositol 4-phosphate and ARF1 GTPase recognition by the FAPP1 pleckstrin homology (PH) domain.
He J, Scott JL, Heroux A, Roy S, Lenoir M, Overduin M, Stahelin RV, Kutateladze TG
J Biol Chem 286 18650-7 (2011)
PMID: 21454700

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-190732 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pleckstrin homology domain-containing family A member 3 Chain: A
Molecule details ›
Chain: A
Length: 103 amino acids
Theoretical weight: 11.99 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9HB20 (Residues: 1-99; Coverage: 33%)
Gene names: FAPP1, PLEKHA3
Sequence domains: PH domain
Structure domains: Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)

Ligands and Environments

1 bound ligand:
Ligand GOL 1 x GOL
1 modified residue:
Ligand MSE 4 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: P41212
Unit cell:
a: 31.025Å b: 31.025Å c: 216.69Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.265 0.23 0.255
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

18 review citations

Phosphoinositides: tiny lipids with giant impact on cell regulation.
Balla T. (2013)
17 more

9 mentions without citation

Emerging methodologies to investigate lipid-protein interactions.
Scott et al. (2012)
8 more