› 3mn3

X-ray diffraction
2.38Å resolution

An inhibited conformation for the protein kinase domain of the Saccharomyces cerevisiae AMPK homolog Snf1

Released:
DOI: 10.2210/pdb3mn3/pdb
PDB entry 3mn3 coloured by chain, front view.
PDB entry 3mn3 coloured by chain, side view.
PDB entry 3mn3 coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
An inhibited conformation for the protein kinase domain of the Saccharomyces cerevisiae AMPK homolog Snf1.
Rudolph MJ, Amodeo GA, Tong L
Acta Crystallogr Sect F Struct Biol Cryst Commun 66 999-1002 (2010)
PMID: 20823513

Function and Biology Details

Reaction catalysed: 
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-139223 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carbon catabolite-derepressing protein kinase Chain: A
Molecule details ›
Chain: A
Length: 271 amino acids
Theoretical weight: 31.03 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P06782 (Residues: 50-320; Coverage: 43%)
Gene names: CAT1, CCR1, D8035.20, GLC2, PAS14, SNF1, YDR477W
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4C
Spacegroup: I4122
Unit cell:
a: 76.981Å b: 76.981Å c: 286.215Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.231 0.23 0.246
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

AMP-activated protein kinase: structure, function, and role in pathological processes.
Novikova et al. (2015)
3 other articles

1 mention without citation

An inhibited conformation for the protein kinase domain of the Saccharomyces cerevisiae AMPK homolog Snf1.
Rudolph et al. (2010)