Research workbench
AlphaFold monomer V2.0 prediction for myelin P2 protein (P02690)
Analyse AlphaFold monomer V2.0 prediction for myelin P2 protein (P02690) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P02690
- Type
- protein
- Length
- 132 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x80E4770D64c852Ea54fa095e4246B7F0d7647117
- Molecule
- Myelin P2 protein
- UniProt
- P02690
- Pockets
- 1 · best druggability 0.83
Structure
1 distinct chain · 14% helix, 59% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Myelin P2 protein | protein | 132 | 14% helix, 59% strand | P02690 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 375 | 0.83 | 0.91 | 37 | empty |
Compared structures
- 1PMP · Crystallographic studies on a family of cellular lipophilic transport proteins.… · an experimental structure of the same protein · chain A against A, TM-score 0.98
- 1PMP · Crystallographic studies on a family of cellular lipophilic transport proteins.… · an experimental structure of the same protein · chain A against A, TM-score 0.98
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 P02690
- Elsewhere: UniProt P02690 · AlphaFold DB P02690
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