Research workbench
AlphaFold monomer V2.0 prediction for DUF21 domain-containing protein AT1G55930, chloroplastic (Q84R21)
Analyse AlphaFold monomer V2.0 prediction for DUF21 domain-containing protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q84R21
- Type
- protein
- Length
- 653 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xA282412EdfcE4C50dd88EF2f60821010627e7F46
- Molecule
- DUF21 domain-containing protein AT1G55930, chloroplastic
- UniProt
- Q84R21
- Pockets
- 4 · best druggability 0.71
Structure
1 distinct chain · 46% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DUF21 domain-containing protein AT1G55930, chloroplastic | protein | 653 | 46% helix, 11% strand | Q84R21 |
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 | 1124 | 0.71 | 0.75 | 67 | empty |
| 2 | 593 | 0.67 | 0.76 | 49 | empty |
| 3 | 181 | 0.54 | 0.79 | 23 | empty |
| 4 | 159 | 0.47 | 0.76 | 19 | 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 Q84R21
- Elsewhere: UniProt Q84R21 · AlphaFold DB Q84R21
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