Research workbench
AlphaFold monomer V2.0 prediction for ATPase family aaa domain- containing protein 3 (Q3KRE0)
Analyse AlphaFold monomer V2.0 prediction for ATPase family aaa domain- containing… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q3KRE0
- Type
- protein
- Length
- 591 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xDAedCe502c997826FD28D12aD4a59b1c3bB855bb
- Molecule
- ATPase family aaa domain-containing protein 3
- UniProt
- Q3KRE0
- Pockets
- 4 · best druggability 0.54
Structure
1 distinct chain · 65% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATPase family aaa domain-containing protein 3 | protein | 591 | 65% helix, 6% strand | Q3KRE0 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 180 | 0.54 | 0.79 | 37 | empty |
| 2 | 237 | 0.51 | 0.75 | 28 | empty |
| 3 | 119 | 0.43 | 0.77 | 21 | empty |
| 4 | 82 | 0.31 | 0.73 | 20 | empty |
Modifications
Observed in the structure: 1 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 Q3KRE0
- Elsewhere: UniProt Q3KRE0 · AlphaFold DB Q3KRE0
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