Research workbench
AlphaFold monomer V2.0 prediction for uncharacterized ring finger membrane protein C15C4.06C (Q1MTR5)
Analyse AlphaFold monomer V2.0 prediction for uncharacterized ring finger membrane… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q1MTR5
- Type
- protein
- Length
- 556 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7c75F0f7d6d136A2b8D4C6C6e9b3D8a697949DF1
- Molecule
- Uncharacterized ring finger membrane protein C15C4.06C
- UniProt
- Q1MTR5
- Pockets
- 2 · best druggability 0.47
Structure
1 distinct chain · 34% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized ring finger membrane protein C15C4.06C | protein | 556 | 34% helix, 13% strand | Q1MTR5 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 202 | 0.47 | 0.75 | 28 | empty |
| 2 | 118 | 0.40 | 0.75 | 15 | empty |
Modifications
Observed in the structure: 2 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 Q1MTR5
- Elsewhere: UniProt Q1MTR5 · AlphaFold DB Q1MTR5
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