› 1nlo

Solution NMR

STRUCTURE OF SIGNAL TRANSDUCTION PROTEIN, NMR, MINIMIZED AVERAGE STRUCTURE

Released:
DOI: 10.2210/pdb1nlo/pdb
PDB entry 1nlo coloured by chain, front view.
PDB entry 1nlo coloured by chain, side view.
PDB entry 1nlo coloured by chain, top view.
Source organism: Gallus gallus
Primary publication:
Molecular basis for the binding of SH3 ligands with non-peptide elements identified by combinatorial synthesis.
Feng S, Kapoor TM, Shirai F, Combs AP, Schreiber SL
Chem Biol 3 661-70 (1996)
PMID: 8807900

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-132632 (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: 7.1 KDa
Source organism: Gallus gallus
Expression system: GST-FUSION
UniProt:
  • Canonical: P00523 (Residues: 77-140; Coverage: 12%)
Gene name: SRC
Sequence domains: SH3 domain
Structure domains: SH3 Domains
NL1 (MN7-MN2-MN1-PLPPLP) Chain: N
Molecule details ›
Chain: N
Length: 11 amino acids
Theoretical weight: 1.15 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 system: Not provided

Quick links

Citations

9 review citations

The importance of being proline: the interaction of proline-rich motifs in signaling proteins with their cognate domains.
Kay et al. (2000)
8 more

4 mentions without citation

Diffusion, crowding & protein stability in a dynamic molecular model of the bacterial cytoplasm.
McGuffee et al. (2010)
3 more