PDBe 4cfe

X-ray diffraction
3.02Å resolution

Structure of full length human AMPK in complex with a small molecule activator, a benzimidazole derivative (991)

Released:

Function and Biology Details

Reactions catalysed:
ATP + [acetyl-CoA carboxylase] = ADP + [acetyl-CoA carboxylase] phosphate
ATP + a protein = ADP + a phosphoprotein
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)] = ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
5'-AMP-activated protein kinase catalytic subunit alpha-2 Chains: A, C
Molecule details ›
Chains: A, C
Length: 571 amino acids
Theoretical weight: 64.65 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P54646 (Residues: 1-552; Coverage: 100%)
Gene names: AMPK, AMPK2, PRKAA2
Sequence domains:
5'-AMP-activated protein kinase subunit beta-1 Chains: B, D
Molecule details ›
Chains: B, D
Length: 286 amino acids
Theoretical weight: 32.45 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Y478 (Residues: 1-270; Coverage: 100%)
Gene names: AMPK, PRKAB1
Sequence domains:
5'-AMP-activated protein kinase subunit gamma-1 Chains: E, F
Molecule details ›
Chains: E, F
Length: 331 amino acids
Theoretical weight: 37.63 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P54619 (Residues: 1-331; Coverage: 100%)
Gene name: PRKAG1
Sequence domains: CBS domain

Ligands and Environments

3 bound ligands:

2 modified residues:

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: P21
Unit cell:
a: 76.03Å b: 134.141Å c: 140.558Å
α: 90° β: 92.42° γ: 90°
R-values:
R R work R free
0.219 0.218 0.253
Expression system: Escherichia coli