PDBe 1spr

X-ray diffraction
2.5Å resolution

BINDING OF A HIGH AFFINITY PHOSPHOTYROSYL PEPTIDE TO THE SRC SH2 DOMAIN: CRYSTAL STRUCTURES OF THE COMPLEXED AND PEPTIDE-FREE FORMS

Released:

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
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine-protein kinase transforming protein Src Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 104 amino acids
Theoretical weight: 11.97 KDa
Source organism: Rous sarcoma virus
Expression system: Not provided
UniProt:
  • Canonical: P00524 (Residues: 144-247; Coverage: 20%)
Gene name: V-SRC
Sequence domains: SH2 domain
Structure domains: SHC Adaptor Protein

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21212
Unit cell:
a: 110.6Å b: 86.2Å c: 58.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.185 0.185 not available
Expression system: Not provided