› 3aqv

X-ray diffraction
2.08Å resolution

Human AMP-activated protein kinase alpha 2 subunit kinase domain (T172D) complexed with compound C

Released:
DOI: 10.2210/pdb3aqv/pdb
PDB entry 3aqv coloured by chain, front view.
PDB entry 3aqv coloured by chain, side view.
PDB entry 3aqv coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for compound C inhibition of the human AMP-activated protein kinase α2 subunit kinase domain.
Handa N, Takagi T, Saijo S, Kishishita S, Takaya D, Toyama M, Terada T, Shirouzu M, Suzuki A, Lee S, Yamauchi T, Okada-Iwabu M, Iwabu M, Kadowaki T, Minokoshi Y, Yokoyama S
Acta Crystallogr D Biol Crystallogr 67 480-7 (2011)
PMID: 21543851

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: 31.57 KDa
Source organism: Homo sapiens
Expression system: Cell-free protein synthesis
UniProt:
  • Canonical: P54646 (Residues: 6-279; Coverage: 50%)
Gene names: AMPK, AMPK2, PRKAA2
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand TAK 1 x TAK
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: P43212
Unit cell:
a: 70.476Å b: 70.476Å c: 130.508Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.224 0.221 0.281
Expression system: Cell-free protein synthesis

Quick links

Citations

10 review citations

The plant energy sensor: evolutionary conservation and divergence of SnRK1 structure, regulation, and function.
Broeckx et al. (2016)
9 more

7 mentions without citation

AMP-activated protein kinase selectively inhibited by the type II inhibitor SBI-0206965.
Dite et al. (2018)
6 more