› 2i5c

X-ray diffraction
1.75Å resolution

Crystal structure of the C-terminal PH domain of pleckstrin in complex with D-myo-Ins(1,2,3,4,5)P5

Released:
DOI: 10.2210/pdb2i5c/pdb
PDB 2i5c coloured by chain and viewed from the front.
PDB 2i5c coloured by chain and viewed from the side.
PDB 2i5c coloured by chain and viewed from the top.
Source organism: Homo sapiens
Primary publication:
Structural analysis of the carboxy terminal PH domain of pleckstrin bound to D-myo-inositol 1,2,3,5,6-pentakisphosphate.
Jackson SG, Zhang Y, Haslam RJ, Junop MS
BMC Struct. Biol. 7 80 (2007)
PMID: 18034889

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pleckstrin Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 109 amino acids
Theoretical weight: 12.45 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P08567 (Residues: 244-347; Coverage: 30%)
Gene names: P47, PLEK
Sequence domains: PH domain
Structure domains: Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)

Ligands and Environments

1 bound ligand:
Ligand IP5 3 x IP5
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X26C
Spacegroup: C2
Unit cell:
a: 82.501Å b: 47.604Å c: 87.622Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.176 0.243
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Computational and theoretical approaches for studies of a lipid recognition protein on biological membranes.
Yamamoto E. (2017)
2 more

4 mentions without citation

Emerging Roles of Pleckstrin-2 Beyond Cell Spreading.
Wang et al. (2021)
3 more