6c4u

X-ray diffraction
2.6Å resolution

Engineered FHA with Myc-pTBD peptide

Released:

Function and Biology Details

Reaction catalysed:
ATP + L-seryl/L-threonyl/L-tyrosyl-[protein] = ADP + O-phospho-L-seryl/O-phospho-L-threonyl/O-phospho-L-tyrosyl-[protein]
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-133945 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine/threonine-protein kinase RAD53 Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 134 amino acids
Theoretical weight: 15.13 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P22216 (Residues: 29-162; Coverage: 16%)
Gene names: MEC2, P2588, RAD53, SAD1, SPK1, YPL153C
Sequence domains: FHA domain
Structure domains: Tumour Suppressor Smad4
Myc proto-oncogene protein Chains: G, H, I, J, K, L
Molecule details ›
Chains: G, H, I, J, K, L
Length: 9 amino acids
Theoretical weight: 1.05 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P01106 (Residues: 69-77; Coverage: 2%)
Gene names: BHLHE39, MYC

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P2221
Unit cell:
a: 70.18Å b: 72.37Å c: 280.35Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.235 0.233 0.279
Expression systems:
  • Escherichia coli
  • Not provided