4u5j

X-ray diffraction
2.26Å resolution

C-Src in complex with Ruxolitinib

Released:
Source organism: Gallus gallus
Primary publication:
c-Src binds to the cancer drug Ruxolitinib with an active conformation.
PLoS One 9 e106225 (2014)
PMID: 25197973

Function and Biology Details

Reaction catalysed:
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-132629 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Proto-oncogene tyrosine-protein kinase Src Chains: A, B
Molecule details ›
Chains: A, B
Length: 286 amino acids
Theoretical weight: 32.73 KDa
Source organism: Gallus gallus
Expression system: Escherichia coli #1/H766
UniProt:
  • Canonical: P00523 (Residues: 251-533; Coverage: 53%)
Gene name: SRC
Sequence domains: Protein tyrosine and serine/threonine kinase
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P1
Unit cell:
a: 42.107Å b: 63.228Å c: 73.989Å
α: 79.27° β: 89.27° γ: 90.29°
R-values:
R R work R free
0.199 0.197 0.236
Expression system: Escherichia coli #1/H766