2ltu

Solution NMR

Solution Structure of autoinhibitory domain of human AMP-activated protein kinase catalytic subunit

Released:
Source organism: Homo sapiens
Entry authors: Xia B, Hu J

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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
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: 62 amino acids
Theoretical weight: 7.03 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P54646 (Residues: 282-339; Coverage: 11%)
Gene names: AMPK, AMPK2, PRKAA2
Sequence domains: AMP-activated protein kinase, alpha subunit, autoinhibitory domain
Structure domains: DNA helicase RuvA subunit, C-terminal domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 85%
Refinement method: simulated annealing
Expression system: Escherichia coli BL21(DE3)