MolNFT v1 · #319843 · protein
AlphaFold monomer V2.0 prediction for receptor-type tyrosine-protein phosphatase epsilon (P23469)
P23469: “AlphaFold monomer V2.0 prediction for receptor-type tyrosine-protein phosphatase epsilon (P23469)”. 9 pockets (best druggability 0.79). MolNFT v1 #319843 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- P23469
- Type
- protein
- Length
- 700 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x79a905d858Ce72991FD6E7a9C6498620f42E146D
- Molecule
- Receptor-type tyrosine-protein phosphatase epsilon
- UniProt
- P23469
- Pockets
- 9 · best druggability 0.79
Structure
1 distinct chain · 36% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Receptor-type tyrosine-protein phosphatase epsilon | protein | 700 | 36% helix, 18% strand | P23469 |
Pockets
9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 331 | 0.79 | 0.89 | 35 | empty |
| 2 | 354 | 0.60 | 0.77 | 29 | empty |
| 3 | 272 | 0.57 | 0.78 | 25 | empty |
| 4 | 81 | 0.54 | 0.85 | 19 | empty |
| 5 | 126 | 0.42 | 0.76 | 22 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 2JJD · Protein tyrosine phosphatase, receptor type, E isoform · an experimental structure of the same protein · chain A against B, TM-score 0.77
- 2JJD · Protein Tyrosine Phosphatase, Receptor Type, E isoform · an experimental structure of the same protein · chain A against B, TM-score 0.77
- 6D4D · Crystal structure of the ptp epsilon D1 domain · an experimental structure of the same protein · chain A against A, TM-score 0.40
- 6D4D · Crystal structure of the PTP epsilon D1 domain · an experimental structure of the same protein · chain A against A, TM-score 0.40
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 P23469
- Elsewhere: UniProt P23469 · AlphaFold DB P23469
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