› 1o4p

X-ray diffraction
1.9Å 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
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 791 1 x 791
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELLIOTT GX-21
Spacegroup: P212121
Unit cell:
a: 26.836Å b: 59.066Å c: 64.922Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.169 0.169 not available
Expression system: Escherichia coli

Quick links

Citations

9 review citations

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

1 mention without citation

Ligand deconstruction: Why some fragment binding positions are conserved and others are not.
Kozakov et al. (2015)