› 1is0

X-ray diffraction
1.9Å resolution

Crystal Structure of a Complex of the Src SH2 Domain with Conformationally Constrained Peptide Inhibitor

Released:
DOI: 10.2210/pdb1is0/pdb
PDB entry 1is0 coloured by chain, front view.
PDB entry 1is0 coloured by chain, side view.
PDB entry 1is0 coloured by chain, top view.
Source organism: Rous sarcoma virus
Primary publication:
Calorimetric and structural studies of 1,2,3-trisubstituted cyclopropanes as conformationally constrained peptide inhibitors of Src SH2 domain binding.
Davidson JP, Lubman O, Rose T, Waksman G, Martin SF
J Am Chem Soc 124 205-15 (2002)
PMID: 11782172

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:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132662 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Tyrosine-protein kinase transforming protein Src Chains: A, B
Molecule details ›
Chains: A, B
Length: 106 amino acids
Theoretical weight: 12.19 KDa
Source organism: Rous sarcoma virus
Expression system: Escherichia coli
UniProt:
  • Canonical: P00524 (Residues: 144-249; Coverage: 20%)
Gene name: V-SRC
Sequence domains: SH2 domain
Structure domains: SH2 domain
AY0 GLU GLU ILE peptide Chains: C, D
Molecule details ›
Chains: C, D
Length: 4 amino acids
Theoretical weight: 687 Da
Source organism: Rous sarcoma virus
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 58.355Å b: 56.501Å c: 69.305Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.236 0.236 0.272
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

4 review citations

Phosphate recognition in structural biology.
Hirsch et al. (2007)
3 more

7 mentions without citation

Constraining binding hot spots: NMR and molecular dynamics simulations provide a structural explanation for enthalpy-entropy compensation in SH2-ligand binding.
Ward et al. (2010)
6 more