4red

X-ray diffraction
2.95Å resolution

Crystal structure of human AMPK alpha1 KD-AID with K43A mutation

Released:

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo tetramer
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-171548 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
5'-AMP-activated protein kinase catalytic subunit alpha-1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 351 amino acids
Theoretical weight: 40.2 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q13131 (Residues: 22-362; Coverage: 61%)
Gene names: AMPK1, PRKAA1
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: I4122
Unit cell:
a: 119.532Å b: 119.532Å c: 215.639Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.233 0.23 0.277
Expression system: Escherichia coli BL21(DE3)