› 1prm

Solution NMR

TWO BINDING ORIENTATIONS FOR PEPTIDES TO SRC SH3 DOMAIN: DEVELOPMENT OF A GENERAL MODEL FOR SH3-LIGAND INTERACTIONS

Released:
DOI: 10.2210/pdb1prm/pdb
PDB entry 1prm coloured by chain, front view.
PDB entry 1prm coloured by chain, side view.
PDB entry 1prm coloured by chain, top view.
Source organism: Gallus gallus
Primary publication:
Two binding orientations for peptides to the Src SH3 domain: development of a general model for SH3-ligand interactions.
Feng S, Chen JK, Yu H, Simon JA, Schreiber SL
Science 266 1241-7 (1994)
PMID: 7526465

Function and Biology Details

Reaction catalysed: 
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132636 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Proto-oncogene tyrosine-protein kinase Src Chain: C
Molecule details ›
Chain: C
Length: 64 amino acids
Theoretical weight: 7 KDa
Source organism: Gallus gallus
Expression system: Escherichia coli
UniProt:
  • Canonical: P00523 (Residues: 77-140; Coverage: 12%)
Gene name: SRC
Sequence domains: SH3 domain
Structure domains: SH3 Domains
PROLINE-RICH LIGAND PLR1 (AFAPPLPRR) Chain: A
Molecule details ›
Chain: A
Length: 9 amino acids
Theoretical weight: 1.03 KDa
Source organism: Gallus gallus
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

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

Quick links

Citations

83 review citations

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

5 mentions without citation

Dynamic regulatory features of the protein tyrosine kinases.
Amatya et al. (2019)
4 more