4pdp

X-ray diffraction
2.59Å resolution

Crystal structure of Rad53 kinase domain and SCD2

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:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-149544 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine/threonine-protein kinase RAD53 Chains: A, B
Molecule details ›
Chains: A, B
Length: 347 amino acids
Theoretical weight: 38.43 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P22216 (Residues: 170-512; Coverage: 42%)
Gene names: MEC2, P2588, RAD53, SAD1, SPK1, YPL153C
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 X29A
Spacegroup: C2221
Unit cell:
a: 76.43Å b: 79.07Å c: 227.71Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.23 0.227 0.261
Expression system: Escherichia coli