4eai

X-ray diffraction
2.28Å resolution

Co-crystal structure of an AMPK core with AMP

Released:

Function and Biology Details

Reactions catalysed:
ATP + a protein = ADP + a phosphoprotein
ATP + [tau protein] = ADP + [tau protein] phosphate
ATP + [acetyl-CoA carboxylase] = ADP + [acetyl-CoA carboxylase] phosphate
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)] = ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
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-1 Chain: A
Molecule details ›
Chain: A
Length: 106 amino acids
Theoretical weight: 12.1 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P54645 (Residues: 405-479, 540-559; Coverage: 17%)
Gene names: Ampk1, Prkaa1
Structure domains: Kinase associated domain 1, KA1
5'-AMP-activated protein kinase subunit beta-2 Chain: B
Molecule details ›
Chain: B
Length: 85 amino acids
Theoretical weight: 9.89 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O43741 (Residues: 189-272; Coverage: 31%)
Gene name: PRKAB2
Sequence domains: 5'-AMP-activated protein kinase beta subunit, interaction domain
5'-AMP-activated protein kinase subunit gamma-1 Chain: C
Molecule details ›
Chain: C
Length: 330 amino acids
Theoretical weight: 37.43 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P80385 (Residues: 1-330; Coverage: 100%)
Gene name: Prkag1
Sequence domains: CBS domain

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P21212
Unit cell:
a: 97.594Å b: 115.334Å c: 48.522Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.194 0.252
Expression system: Escherichia coli