Research workbench
Fyn SH2 domain in complex with the natural inhibitory phosphotyrosine peptide
Analyse Fyn SH2 domain in complex with the natural inhibitory phosphotyrosine peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2MRK
- Type
- protein
- Length
- 110 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tyrosine-protein kinase fyn; C-terminal tyrosine-protein kinase fyn
- EC
- 2.7.10.2
- UniProt
- P06241
Structure
solution nmr · 2 distinct chains · 13% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosine-protein kinase fyn (EC 2.7.10.2) | protein | 100 | 14% helix, 21% strand | P06241 |
| B | C-terminal tyrosine-protein kinase fyn (EC 2.7.10.2) | protein | 10 | 0% helix, 0% strand | P06241 |
Interfaces
1 interface between chains.
- A–B · 493 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (phosphorylation).
Compared structures
- 2MRK · Fyn SH2 domain in complex with the natural inhibitory phosphotyrosine peptide · the same entry in another collection · chain A against A, TM-score 1.00
- P06241 · AlphaFold monomer V2.0 prediction for tyrosine-protein kinase fyn (P06241) · a predicted model of the same protein · chain A against A, TM-score 0.85
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P06241
- Elsewhere: RCSB PDB 2MRK · PDBe 2MRK · UniProt P06241
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