Research workbench
AlphaFold monomer V2.0 prediction for D-tagatose-1,6-bisphosphate aldolase subunit kbaz (B7LMV1)
Analyse AlphaFold monomer V2.0 prediction for D-tagatose-1,6-bisphosphate aldolase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B7LMV1
- Type
- protein
- Length
- 426 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x8c2D56B87823aE0eC22a00C7d67B25Fa307D4d29
- Molecule
- D-tagatose-1,6-bisphosphate aldolase subunit kbaz
- UniProt
- B7LMV1
- Pockets
- 6 · best druggability 0.69
Structure
1 distinct chain · 53% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | D-tagatose-1,6-bisphosphate aldolase subunit kbaz | protein | 426 | 53% helix, 10% strand | B7LMV1 |
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 204 | 0.69 | 0.86 | 43 | empty |
| 2 | 100 | 0.49 | 0.81 | 15 | empty |
| 3 | 118 | 0.38 | 0.74 | 19 | empty |
| 4 | 107 | 0.35 | 0.73 | 21 | empty |
| 5 | 53 | 0.31 | 0.76 | 13 | 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 B7LMV1
- Elsewhere: UniProt B7LMV1 · AlphaFold DB B7LMV1
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