PDBe 1qwe

Solution NMR

C-SRC SH3 DOMAIN COMPLEXED WITH LIGAND APP12

Released:
Primary publication:
Specific interactions outside the proline-rich core of two classes of Src homology 3 ligands.
Proc. Natl. Acad. Sci. U.S.A. 92 12408-15 (1995)
PMID: 8618911

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):
ALA-PRO-PRO-LEU-PRO-PRO-ARG-ASN-ARG-PRO-ARG-LEU Chain: B
Molecule details ›
Chain: B
Length: 12 amino acids
Theoretical weight: 1.39 KDa
Source organism: Unidentified
Expression system: Not provided
Tyrosine-protein kinase transforming protein Src Chain: A
Molecule details ›
Chain: A
Length: 64 amino acids
Theoretical weight: 7.1 KDa
Source organism: Avian sarcoma virus
Expression system: Escherichia coli
UniProt:
  • Canonical: P00525 (Residues: 77-140; Coverage: 12%)
Gene name: V-SRC
Sequence domains: SH3 domain
Structure domains: SH3 Domains

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Expression systems:
  • Not provided
  • Escherichia coli