Research workbench
AlphaFold monomer V2.0 prediction for maturase K (B1A916)
Analyse AlphaFold monomer V2.0 prediction for maturase K (B1A916) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B1A916
- Type
- protein
- Length
- 506 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x71112d4fF7ebb3b617963c05f052289e073082FD
- Molecule
- Maturase K
- UniProt
- B1A916
- Pockets
- 11 · best druggability 0.73
Structure
1 distinct chain · 52% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Maturase K | protein | 506 | 52% helix, 11% strand | B1A916 |
Pockets
11 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 76 | 0.73 | 0.96 | 21 | empty |
| 2 | 757 | 0.72 | 0.77 | 66 | empty |
| 3 | 448 | 0.68 | 0.79 | 38 | empty |
| 4 | 372 | 0.64 | 0.79 | 37 | empty |
| 5 | 467 | 0.63 | 0.76 | 34 | 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 B1A916
- Elsewhere: UniProt B1A916 · AlphaFold DB B1A916
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