› 4a5k

X-ray diffraction
1.76Å resolution

Structural analyses of Slm1-PH domain demonstrate ligand binding in the non-canonical site

Released:
DOI: 10.2210/pdb4a5k/pdb
PDB entry 4a5k coloured by chain, front view.
PDB entry 4a5k coloured by chain, side view.
PDB entry 4a5k coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Structural analyses of the Slm1-PH domain demonstrate ligand binding in the non-canonical site.
Anand K, Maeda K, Gavin AC
PLoS One 7 e36526 (2012)
PMID: 22574179

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-154127 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphatidylinositol 4,5-bisphosphate-binding protein SLM1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 118 amino acids
Theoretical weight: 13.52 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P40485 (Residues: 469-583; Coverage: 17%)
Gene names: LIT2, SLM1, YIL105C
Sequence domains: PH domain
Structure domains: Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)

Ligands and Environments

1 bound ligand:
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P21
Unit cell:
a: 37.3Å b: 82.3Å c: 76.4Å
α: 90° β: 90.1° γ: 90°
R-values:
R R work R free
0.189 0.188 0.227
Expression system: Escherichia coli BL21

Quick links

Citations

3 review citations

Polyphosphoinositide-Binding Domains: Insights from Peripheral Membrane and Lipid-Transfer Proteins.
Pemberton et al. (2019)
2 more

2 mentions without citation

Structural analyses of the Slm1-PH domain demonstrate ligand binding in the non-canonical site.
Anand et al. (2012)
1 more