› 2h6d

X-ray diffraction
1.85Å resolution

Protein Kinase Domain of the Human 5'-AMP-activated protein kinase catalytic subunit alpha-2 (AMPK alpha-2 chain)

Released:
DOI: 10.2210/pdb2h6d/pdb
PDB entry 2h6d coloured by chain, front view.
PDB entry 2h6d coloured by chain, side view.
PDB entry 2h6d coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
A conserved mechanism of autoinhibition for the AMPK kinase domain: ATP-binding site and catalytic loop refolding as a means of regulation.
Littler DR, Walker JR, Davis T, Wybenga-Groot LE, Finerty PJ, Newman E, Mackenzie F, Dhe-Paganon S
Acta Crystallogr Sect F Struct Biol Cryst Commun 66 143-51 (2010)
PMID: 20124709

Function and Biology Details

Reactions catalysed: 
ATP + a protein = ADP + a phosphoprotein
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)] = ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157068 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
5'-AMP-activated protein kinase catalytic subunit alpha-2 Chain: A
Molecule details ›
Chain: A
Length: 276 amino acids
Theoretical weight: 31.56 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P54646 (Residues: 6-279; Coverage: 50%)
Gene names: AMPK, AMPK2, PRKAA2
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21
Unit cell:
a: 39.454Å b: 67.41Å c: 50.493Å
α: 90° β: 91.3° γ: 90°
R-values:
R R work R free
0.19 0.188 0.227
Expression system: Escherichia coli BL21

Quick links

Citations

5 review citations

Roles of AMP-activated protein kinase in Alzheimer's disease.
Cai et al. (2012)
4 more

16 mentions without citation

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