› 1p13

X-ray diffraction
1.63Å resolution

Crystal Structure of the Src SH2 Domain Complexed with Peptide (SDpYANFK)

Released:
DOI: 10.2210/pdb1p13/pdb
PDB entry 1p13 coloured by chain, front view.
PDB entry 1p13 coloured by chain, side view.
PDB entry 1p13 coloured by chain, top view.
Source organism: Gallus gallus
Primary publication:
The structure of the membrane distal phosphatase domain of RPTPalpha reveals interdomain flexibility and an SH2 domain interaction region.
Sonnenburg ED, Bilwes A, Hunter T, Noel JP
Biochemistry 42 7904-14 (2003)
PMID: 12834342

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-132634 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Proto-oncogene tyrosine-protein kinase Src Chains: A, B
Molecule details ›
Chains: A, B
Length: 102 amino acids
Theoretical weight: 11.74 KDa
Source organism: Gallus gallus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P00523 (Residues: 145-246; Coverage: 19%)
Gene name: SRC
Sequence domains: SH2 domain
Structure domains: SH2 domain
Peptide Chains: C, D
Molecule details ›
Chains: C, D
Length: 7 amino acids
Theoretical weight: 941 Da
Source organism: Gallus gallus
Expression system: Not provided

Ligands and Environments

1 bound ligand:
Ligand CAC 4 x CAC
1 modified residue:
Ligand PTR 2 x PTR

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: P212121
Unit cell:
a: 58.384Å b: 58.793Å c: 62.662Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.252 0.207 0.252
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

7 review citations

Src kinase regulation by phosphorylation and dephosphorylation.
Roskoski R. (2005)
6 more

196 mentions without citation

The ADAM metalloproteinases.
Edwards et al. (2008)
195 more