PDBe 1sps

X-ray diffraction
2.7Å 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:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Middle T antigen Chains: D, E, F
Molecule details ›
Chains: D, E, F
Length: 11 amino acids
Theoretical weight: 1.47 KDa
Source organism: Mesocricetus auratus polyomavirus 1
Expression system: Not provided
UniProt:
  • Canonical: P03079 (Residues: 321-331; Coverage: 3%)
Tyrosine-protein kinase transforming protein Src Chains: A, B, C
Molecule details ›
Chains: A, B, C
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

No bound ligands

1 modified residue:

Experiments and Validation Details

Entry percentile scores
Spacegroup: P41
Unit cell:
a: 93.3Å b: 93.3Å c: 55Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.18 not available
Expression system: Not provided