Research workbench
AlphaFold monomer V2.0 prediction for histidine biosynthesis bifunctional protein hisb (Q6D409)
Analyse AlphaFold monomer V2.0 prediction for histidine biosynthesis bifunctional… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q6D409
- Type
- protein
- Length
- 355 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4Ef77Afb5a3D9F41c95Be3227D1CC986CCb61835
- Molecule
- Histidine biosynthesis bifunctional protein hisb
- UniProt
- Q6D409
- Pockets
- 3 · best druggability 0.44
Structure
1 distinct chain · 36% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histidine biosynthesis bifunctional protein hisb | protein | 355 | 36% helix, 26% strand | Q6D409 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 79 | 0.44 | 0.81 | 18 | empty |
| 2 | 78 | 0.31 | 0.73 | 16 | empty |
| 3 | 76 | 0.28 | 0.72 | 18 | 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 Q6D409
- Elsewhere: UniProt Q6D409 · AlphaFold DB Q6D409
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