Research workbench
AlphaFold monomer V2.0 prediction for protein MPE1 (P35728)
Analyse AlphaFold monomer V2.0 prediction for protein MPE1 (P35728) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P35728
- Type
- protein
- Length
- 441 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5881B09f2D8e743400698633641fc1cD2Ed2BE6F
- Molecule
- Protein MPE1
- UniProt
- P35728
- Pockets
- 4 · best druggability 0.33
Structure
1 distinct chain · 26% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein MPE1 | protein | 441 | 26% helix, 13% strand | P35728 |
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 84 | 0.33 | 0.73 | 12 | empty |
| 2 | 72 | 0.32 | 0.74 | 19 | empty |
| 3 | 51 | 0.29 | 0.76 | 11 | empty |
| 4 | 51 | 0.26 | 0.73 | 14 | empty |
Compared structures
- 6I1D · Structure of the YSH1-MPE1 nuclease complex from S.CEREVISIAE · an experimental structure of the same protein · chain A against B, TM-score 0.20
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 P35728
- Elsewhere: UniProt P35728 · AlphaFold DB P35728
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