MolNFT v1 · #498561 · protein
AlphaFold monomer V2.0 prediction for vitamin D-binding protein (Q3MHN5)
Q3MHN5: “AlphaFold monomer V2.0 prediction for vitamin D-binding protein (Q3MHN5)”. 10 pockets (best druggability 0.74). MolNFT v1 #498561 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- Q3MHN5
- Type
- protein
- Length
- 474 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xc5F2d4623921daC77B95D847de4564f2A1ec9016
- Molecule
- Vitamin D-binding protein
- UniProt
- Q3MHN5
- Pockets
- 10 · best druggability 0.74
Structure
1 distinct chain · 72% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Vitamin D-binding protein | protein | 474 | 72% helix, 0% strand | Q3MHN5 |
Pockets
10 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 62 | 0.74 | 0.98 | 14 | empty |
| 2 | 694 | 0.71 | 0.78 | 63 | empty |
| 3 | 136 | 0.49 | 0.79 | 27 | empty |
| 4 | 173 | 0.49 | 0.76 | 22 | empty |
| 5 | 93 | 0.44 | 0.79 | 19 | empty |
Modifications
Observed in the structure: 14 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 Q3MHN5
- Elsewhere: UniProt Q3MHN5 · AlphaFold DB Q3MHN5
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