Research workbench
AlphaFold monomer V2.0 prediction for B3 domain-containing protein LOC_OS12G40090 (Q2QMT5)
Analyse AlphaFold monomer V2.0 prediction for B3 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
- Q2QMT5
- Type
- protein
- Length
- 334 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xEa58c7534E5701aA8370E0fAEb19b7e14653e69c
- Molecule
- B3 domain-containing protein LOC_OS12G40090
- UniProt
- Q2QMT5
- Pockets
- 3 · best druggability 0.61
Structure
1 distinct chain · 16% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | B3 domain-containing protein LOC_OS12G40090 | protein | 334 | 16% helix, 28% strand | Q2QMT5 |
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 | 315 | 0.61 | 0.78 | 48 | empty |
| 2 | 68 | 0.45 | 0.83 | 16 | empty |
| 3 | 71 | 0.28 | 0.72 | 16 | 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 Q2QMT5
- Elsewhere: UniProt Q2QMT5 · AlphaFold DB Q2QMT5
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