› 1o46

X-ray diffraction
2Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146379 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Proto-oncogene tyrosine-protein kinase Src Chain: A
Molecule details ›
Chain: A
Length: 108 amino acids
Theoretical weight: 12.37 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P12931 (Residues: 145-252; Coverage: 20%)
Gene names: SRC, SRC1
Sequence domains: SH2 domain
Structure domains: SH2 domain

Ligands and Environments

1 bound ligand:
Ligand 903 1 x 903
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELLIOTT GX-21
Spacegroup: P212121
Unit cell:
a: 26.587Å b: 58.554Å c: 64.188Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.192 not available
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

9 review citations

A decade of fragment-based drug design: strategic advances and lessons learned.
Hajduk et al. (2007)
8 more

2 mentions without citation

Dissecting the Influence of Protein Flexibility on the Location and Thermodynamic Profile of Explicit Water Molecules in Protein-Ligand Binding.
Yang et al. (2016)
1 more