› 2f9g

X-ray diffraction
2.1Å resolution

Crystal structure of Fus3 phosphorylated on Tyr182

Released:
DOI: 10.2210/pdb2f9g/pdb
PDB entry 2f9g coloured by chain, front view.
PDB entry 2f9g coloured by chain, side view.
PDB entry 2f9g coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
The Ste5 scaffold allosterically modulates signaling output of the yeast mating pathway.
Bhattacharyya RP, Reményi A, Good MC, Bashor CJ, Falick AM, Lim WA
Science 311 822-6 (2006)
PMID: 16424299

Function and Biology Details

Reaction catalysed: 
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147833 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mitogen-activated protein kinase FUS3 Chain: A
Molecule details ›
Chain: A
Length: 353 amino acids
Theoretical weight: 40.91 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P16892 (Residues: 1-353; Coverage: 100%)
Gene names: DAC2, FUS3, YBL016W, YBL03.21, YBL0303
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand MG 1 x MG
Ligand ADP 1 x ADP
1 modified residue:
Ligand PTR 1 x PTR

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P212121
Unit cell:
a: 56.811Å b: 62.533Å c: 86.008Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.211 0.211 0.26
Expression system: Escherichia coli

Quick links

Citations

49 review citations

Mechanisms of specificity in protein phosphorylation.
Ubersax et al. (2007)
48 more

1 mention without citation

Engineering allosteric regulation in protein kinases.
Pincus et al. (2018)