› 2mrj

Solution NMR

Structure of Fyn protein SH2 bound

Released:
DOI: 10.2210/pdb2mrj/pdb
PDB entry 2mrj coloured by chain, ensemble of 18 models, front view.
PDB entry 2mrj coloured by chain, ensemble of 18 models, side view.
PDB entry 2mrj coloured by chain, ensemble of 18 models, top view.
Source organism: Homo sapiens
Primary publication:
Dynamically Coupled Residues within the SH2 Domain of FYN Are Key to Unlocking Its Activity.
Huculeci R, Cilia E, Lyczek A, Buts L, Houben K, Seeliger MA, van Nuland N, Lenaerts T
Structure 24 1947-1959 (2016)
PMID: 27692963

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 analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-529542 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine-protein kinase Fyn Chain: A
Molecule details ›
Chain: A
Length: 112 amino acids
Theoretical weight: 12.93 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P06241 (Residues: 148-248; Coverage: 19%)
Gene name: FYN
Sequence domains: SH2 domain
Structure domains: SH2 domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 89%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Dynamic regulatory features of the protein tyrosine kinases.
Amatya et al. (2019)
5 other articles