Research workbench
AlphaFold monomer V2.0 prediction for nodulation protein D 1 (P50323)
Analyse AlphaFold monomer V2.0 prediction for nodulation protein D 1 (P50323) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P50323
- Type
- protein
- Length
- 314 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x40B9C9d5F084D34d026E9d5Dd10501AcdF6d6152
- Molecule
- Nodulation protein D 1
- UniProt
- P50323
- Pockets
- 5 · best druggability 0.65
Structure
1 distinct chain · 44% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nodulation protein D 1 | protein | 314 | 44% helix, 22% strand | P50323 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 112 | 0.65 | 0.88 | 22 | empty |
| 2 | 176 | 0.44 | 0.74 | 27 | empty |
| 3 | 171 | 0.42 | 0.73 | 25 | empty |
| 4 | 51 | 0.32 | 0.77 | 10 | empty |
| 5 | 65 | 0.28 | 0.73 | 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 P50323
- Elsewhere: UniProt P50323 · AlphaFold DB P50323
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