MolNFT v1 · #319853 · protein
AlphaFold monomer V2.0 prediction for receptor-type tyrosine-protein phosphatase gamma (Q05909)
Q05909: “AlphaFold monomer V2.0 prediction for receptor-type tyrosine-protein phosphatase gamma (Q05909)”. 20 pockets (best druggability 0.80). MolNFT v1 #319853 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- Q05909
- Type
- protein
- Length
- 1,442 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x13D0a95FDcd918ebb5150FD2C57cfC72eC29DA05
- Molecule
- Receptor-type tyrosine-protein phosphatase gamma
- UniProt
- Q05909
- Pockets
- 20 · best druggability 0.80
Structure
1 distinct chain · 22% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Receptor-type tyrosine-protein phosphatase gamma | protein | 1442 | 22% helix, 19% strand | Q05909 |
Pockets
20 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 118 | 0.80 | 0.99 | 21 | empty |
| 2 | 327 | 0.73 | 0.86 | 38 | empty |
| 3 | 931 | 0.73 | 0.77 | 67 | empty |
| 4 | 304 | 0.70 | 0.84 | 53 | empty |
| 5 | 190 | 0.62 | 0.83 | 25 | empty |
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 5E5U · Crystal structure of the complex between carbonic anhydrase-like domain of ptprg and… · an experimental structure of the same protein · chain A against A, TM-score 0.18
- 3JXG · Ca-like domain of mouse ptprg · an experimental structure of the same protein · chain A against C, TM-score 0.18
- 3JXG · CA-like domain of mouse PTPRG · an experimental structure of the same protein · chain A against C, TM-score 0.18
- 3KLD · Ptprg CNTN4 complex · an experimental structure of the same protein · chain A against B, TM-score 0.18
- 3KLD · PTPRG CNTN4 complex · an experimental structure of the same protein · chain A against B, TM-score 0.18
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 Q05909
- Elsewhere: UniProt Q05909 · AlphaFold DB Q05909
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