Research workbench
AlphaFold monomer V2.0 prediction for nucleoside triphosphate pyrophosphatase (B2HEK5)
Analyse AlphaFold monomer V2.0 prediction for nucleoside triphosphate pyrophosphatase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B2HEK5
- Type
- protein
- Length
- 216 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xBF0D2e107Ce1EcD2C4369B042274201DB719AaAF
- Molecule
- Nucleoside triphosphate pyrophosphatase
- UniProt
- B2HEK5
- Pockets
- 3 · best druggability 0.58
Structure
1 distinct chain · 44% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nucleoside triphosphate pyrophosphatase | protein | 216 | 44% helix, 26% strand | B2HEK5 |
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 | 174 | 0.58 | 0.81 | 36 | empty |
| 2 | 53 | 0.45 | 0.84 | 13 | empty |
| 3 | 59 | 0.28 | 0.74 | 14 | 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 B2HEK5
- Elsewhere: UniProt B2HEK5 · AlphaFold DB B2HEK5
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