Research workbench
AlphaFold monomer V2.0 prediction for zinc finger ccch domain- containing protein 15 (Q1RMM1)
Analyse AlphaFold monomer V2.0 prediction for zinc finger ccch domain- containing… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q1RMM1
- Type
- protein
- Length
- 426 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7a1388B6Aad67B04634A32f63b8A6D6005eab86c
- Molecule
- Zinc finger ccch domain-containing protein 15
- UniProt
- Q1RMM1
- Pockets
- 3 · best druggability 0.53
Structure
1 distinct chain · 47% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Zinc finger ccch domain-containing protein 15 | protein | 426 | 47% helix, 1% strand | Q1RMM1 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 301 | 0.53 | 0.75 | 34 | empty |
| 2 | 53 | 0.37 | 0.80 | 13 | empty |
| 3 | 54 | 0.26 | 0.74 | 11 | empty |
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 Q1RMM1
- Elsewhere: UniProt Q1RMM1 · AlphaFold DB Q1RMM1
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