Research workbench
AlphaFold monomer V2.0 prediction for receptor-type tyrosine-protein phosphatase U (Q92729)
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
- Q92729
- Type
- protein
- Length
- 1,446 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4d07E6a23DeB6B95bd9b90EcB67368b7e8D3B77e
- Molecule
- Receptor-type tyrosine-protein phosphatase U
- UniProt
- Q92729
- Pockets
- 11 · best druggability 0.77
Structure
1 distinct chain · 19% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Receptor-type tyrosine-protein phosphatase U | protein | 1446 | 19% helix, 32% strand | Q92729 |
Pockets
11 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 957 | 0.77 | 0.79 | 94 | empty |
| 2 | 544 | 0.67 | 0.77 | 47 | empty |
| 3 | 149 | 0.57 | 0.82 | 28 | empty |
| 4 | 219 | 0.50 | 0.75 | 31 | empty |
| 5 | 189 | 0.45 | 0.74 | 24 | empty |
Modifications
Observed in the structure: 7 disulfide (disulfide).
Compared structures
- 6SUB · Human ptpru D1 domain, reduced form · an experimental structure of the same protein · chain A against A, TM-score 0.17
- 6SUB · Human PTPRU D1 domain, reduced form · an experimental structure of the same protein · chain A against A, TM-score 0.17
- 6SUC · Human ptpru D1 domain, oxidised form · an experimental structure of the same protein · chain A against A, TM-score 0.16
- 6SUC · Human PTPRU D1 domain, oxidised form · an experimental structure of the same protein · chain A against A, TM-score 0.16
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 Q92729
- Elsewhere: UniProt Q92729 · AlphaFold DB Q92729
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