Research workbench
AlphaFold monomer V2.0 prediction for lysm domain-containing gpi- anchored protein 1 (Q93ZH0)
Analyse AlphaFold monomer V2.0 prediction for lysm domain-containing gpi- anchored… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q93ZH0
- Type
- protein
- Length
- 416 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xb1c9f54629255bE8b3D28b82eAf097a839342609
- Molecule
- Lysm domain-containing gpi-anchored protein 1
- UniProt
- Q93ZH0
- Pockets
- 4 · best druggability 0.69
Structure
1 distinct chain · 19% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lysm domain-containing gpi-anchored protein 1 | protein | 416 | 19% helix, 29% strand | Q93ZH0 |
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 692 | 0.69 | 0.77 | 83 | empty |
| 2 | 200 | 0.56 | 0.79 | 27 | empty |
| 3 | 196 | 0.54 | 0.78 | 27 | empty |
| 4 | 79 | 0.34 | 0.75 | 21 | empty |
Modifications
Observed in the structure: 8 disulfide (disulfide).
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 Q93ZH0
- Elsewhere: UniProt Q93ZH0 · AlphaFold DB Q93ZH0
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