Research workbench
AlphaFold monomer V2.0 prediction for receptor-type tyrosine-protein phosphatase F (A2A8L5)
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
- A2A8L5
- Type
- protein
- Length
- 1,898 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7FDF8b382C6a36A8772D1A265E8e480c7DF0A9C1
- Molecule
- Receptor-type tyrosine-protein phosphatase F
- UniProt
- A2A8L5
- Pockets
- 20 · best druggability 0.77
Structure
1 distinct chain · 14% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Receptor-type tyrosine-protein phosphatase F | protein | 1898 | 14% helix, 38% strand | A2A8L5 |
Pockets
20 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 191 | 0.77 | 0.93 | 25 | empty |
| 2 | 860 | 0.74 | 0.78 | 58 | empty |
| 3 | 434 | 0.67 | 0.79 | 27 | empty |
| 4 | 249 | 0.64 | 0.82 | 23 | empty |
| 5 | 347 | 0.62 | 0.78 | 40 | empty |
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 3PXH · Tandem Ig domains of tyrosine phosphatase LAR · an experimental structure of the same protein · chain A against A, TM-score 0.10
- 3PXH · Tandem ig domains of tyrosine phosphatase lar · an experimental structure of the same protein · chain A against A, TM-score 0.10
- 6X39 · Crystal structure of the FN5 domain of mouse lar · an experimental structure of the same protein · chain A against A, TM-score 0.05
- 6X39 · Crystal structure of the FN5 domain of Mouse Lar · an experimental structure of the same protein · chain A against A, TM-score 0.05
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 A2A8L5
- Elsewhere: UniProt A2A8L5 · AlphaFold DB A2A8L5
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