Research workbench
NMR study of the SH3 domain from fyn proto-oncogene tyrosine kinase, family of 20 structures
Analyse NMR study of the SH3 domain from fyn proto-oncogene tyrosine kinase, family of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1NYG
- Type
- protein
- Length
- 58 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fyn
- EC
- 2.7.1.112
- UniProt
- P06241
Structure
solution nmr · 1 distinct chain · 5% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fyn (EC 2.7.1.112) | protein | 58 | 5% helix, 45% strand | P06241 |
Compared structures
- 1NYG · NMR study of the SH3 domain from fyn proto-oncogene tyrosine kinase, family of 20… · 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 0.89
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 1NYG · PDBe 1NYG · UniProt P06241
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