Research workbench
AlphaFold monomer V2.0 prediction for NAD-capped RNA hydrolase nudc (B5F1H9)
Analyse AlphaFold monomer V2.0 prediction for NAD-capped RNA hydrolase nudc (B5F1H9) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B5F1H9
- Type
- protein
- Length
- 257 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9512b297e46c759A24813dae7167C0c49EF1E7fB
- Molecule
- NAD-capped RNA hydrolase nudc
- UniProt
- B5F1H9
- Pockets
- 3 · best druggability 0.65
Structure
1 distinct chain · 23% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NAD-capped RNA hydrolase nudc | protein | 257 | 23% helix, 38% strand | B5F1H9 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 392 | 0.65 | 0.78 | 30 | empty |
| 2 | 105 | 0.45 | 0.79 | 18 | empty |
| 3 | 99 | 0.42 | 0.77 | 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 B5F1H9
- Elsewhere: UniProt B5F1H9 · AlphaFold DB B5F1H9
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