› 1gzk

X-ray diffraction
2.3Å resolution

Molecular mechanism for the regulation of protein kinase B/Akt by hydrophobic motif phosphorylation

Released:
DOI: 10.2210/pdb1gzk/pdb
PDB entry 1gzk coloured by chain, front view.
PDB entry 1gzk coloured by chain, side view.
PDB entry 1gzk coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Molecular mechanism for the regulation of protein kinase B/Akt by hydrophobic motif phosphorylation.
Yang J, Cron P, Thompson V, Good VM, Hess D, Hemmings BA, Barford D
Mol Cell 9 1227-40 (2002)
PMID: 12086620

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152087 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
RAC-beta serine/threonine-protein kinase Chain: A
Molecule details ›
Chain: A
Length: 315 amino acids
Theoretical weight: 36.49 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P31751 (Residues: 146-460; Coverage: 66%)
Gene name: AKT2
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P41212
Unit cell:
a: 148.405Å b: 148.405Å c: 38.547Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.248 0.248 0.319
Expression system: Spodoptera frugiperda

Quick links

Citations

62 review citations

The nuts and bolts of AGC protein kinases.
Pearce et al. (2010)
61 more

9 mentions without citation

Substrate and docking interactions in serine/threonine protein kinases.
Goldsmith et al. (2007)
8 more