› 1h10

X-ray diffraction
1.4Å resolution

HIGH RESOLUTION STRUCTURE OF THE PLECKSTRIN HOMOLOGY DOMAIN OF PROTEIN KINASE B/AKT BOUND TO INS(1,3,4,5)-TETRAKISPHOPHATE

Released:
DOI: 10.2210/pdb1h10/pdb
PDB entry 1h10 coloured by chain, front view.
PDB entry 1h10 coloured by chain, side view.
PDB entry 1h10 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
High-resolution structure of the pleckstrin homology domain of protein kinase b/akt bound to phosphatidylinositol (3,4,5)-trisphosphate.
Thomas CC, Deak M, Alessi DR, van Aalten DM
Curr Biol 12 1256-62 (2002)
PMID: 12176338

Function and Biology Details

Reaction catalysed: 
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152081 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
RAC-alpha serine/threonine-protein kinase Chain: A
Molecule details ›
Chain: A
Length: 125 amino acids
Theoretical weight: 14.94 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P31749 (Residues: 1-123; Coverage: 26%)
Gene names: AKT1, PKB, RAC
Sequence domains: PH domain
Structure domains: Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)

Ligands and Environments

1 bound ligand:
Ligand 4IP 1 x 4IP
1 modified residue:
Ligand MSE 3 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX14.2
Spacegroup: C2
Unit cell:
a: 82.868Å b: 34.351Å c: 44.293Å
α: 90° β: 115.31° γ: 90°
R-values:
R R work R free
0.125 not available 0.176
Expression system: Escherichia coli BL21

Quick links

Citations

43 review citations

The activation of Akt/PKB signaling pathway and cell survival.
Song et al. (2005)
42 more

78 mentions without citation

Translation of the phosphoinositide code by PI effectors.
Kutateladze TG. (2010)
77 more