› 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:
DOI: 10.2210/pdb1spr/pdb
PDB entry 1spr coloured by chain, front view.
PDB entry 1spr coloured by chain, side view.
PDB entry 1spr coloured by chain, top view.
Source organism: Rous sarcoma virus
Primary publication:
Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: crystal structures of the complexed and peptide-free forms.
Waksman G, Shoelson SE, Pant N, Cowburn D, Kuriyan J
Cell 72 779-90 (1993)
PMID: 7680960

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-132659 (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: SH2 domain

Ligands and Environments

1 bound ligand:
Ligand PO4 1 x PO4
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

Quick links

Citations

92 review citations

Cellular functions regulated by Src family kinases.
Thomas et al. (1997)
91 more

4 mentions without citation

Protein folding: defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins.
Maxwell et al. (2005)
3 more