Research workbench
AlphaFold monomer V2.0 prediction for receptor-type tyrosine-protein phosphatase V (Q64612)
Analyse AlphaFold monomer V2.0 prediction for receptor-type tyrosine-protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q64612
- Type
- protein
- Length
- 1,711 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9B130d619fCFc21d0D08E5Ce38Cf42A5fbe230CB
- Molecule
- Receptor-type tyrosine-protein phosphatase V
- UniProt
- Q64612
- Pockets
- 17 · best druggability 0.70
Structure
1 distinct chain · 15% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Receptor-type tyrosine-protein phosphatase V | protein | 1711 | 15% helix, 39% strand | Q64612 |
Pockets
17 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 255 | 0.70 | 0.85 | 35 | empty |
| 2 | 217 | 0.58 | 0.80 | 32 | empty |
| 3 | 418 | 0.55 | 0.73 | 46 | empty |
| 4 | 166 | 0.52 | 0.79 | 25 | empty |
| 5 | 291 | 0.52 | 0.74 | 33 | empty |
Modifications
Observed in the structure: 4 disulfide (disulfide).
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 Q64612
- Elsewhere: UniProt Q64612 · AlphaFold DB Q64612
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