Research workbench
AlphaFold monomer V2.0 prediction for tyrosine-protein kinase fer (P16591)
Analyse AlphaFold monomer V2.0 prediction for tyrosine-protein kinase fer (P16591) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P16591
- Type
- protein
- Length
- 822 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5c4adF1416281C09AE8eE1cbb80fF7e44cE86F97
- UniProt
- P16591
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 822 | — | P16591 |
Compared structures
- 2KK6 · Solution structure of SH2 domain of proto-oncogene tyrosine-protein kinase fer from homo… · an experimental structure of the same protein · chain A against A, TM-score 0.13
- 2KK6 · Solution structure of sh2 domain of proto-oncogene tyrosine-protein kinase fer from homo… · an experimental structure of the same protein · chain A against A, TM-score 0.13
- 6KC4 · Crystal structure of human fer SH2 domain bound to a phosphopeptide (depyenvd) · an experimental structure of the same protein · chain A against E, TM-score 0.12
- 6KC4 · Crystal structure of human Fer SH2 domain bound to a phosphopeptide (DEpYENVD) · an experimental structure of the same protein · chain A against E, TM-score 0.12
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 P16591
- Elsewhere: UniProt P16591 · AlphaFold DB P16591
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