Research workbench
AlphaFold monomer V2.0 prediction for U3 small nucleolar RNA- associated protein 15 homolog (Q8TED0)
Analyse AlphaFold monomer V2.0 prediction for U3 small nucleolar RNA- associated… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q8TED0
- Type
- protein
- Length
- 518 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5c4adF1416281C09AE8eE1cbb80fF7e44cE86F97
- Molecule
- U3 small nucleolar RNA-associated protein 15 homolog
- UniProt
- Q8TED0
- Pockets
- 2 · best druggability 0.79
Structure
1 distinct chain · 26% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | U3 small nucleolar RNA-associated protein 15 homolog | protein | 518 | 26% helix, 31% strand | Q8TED0 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 654 | 0.79 | 0.84 | 55 | empty |
| 2 | 64 | 0.30 | 0.73 | 15 | empty |
Compared structures
- 7MQ8 · Cryo-EM structure of the human SSU processome, state pre-A1 · an experimental structure of the same protein · chain A against LJ, TM-score 0.74
- 7MQ9 · Cryo-EM structure of the human SSU processome, state pre-A1* · an experimental structure of the same protein · chain A against LJ, TM-score 0.73
- 7MQA · Cryo-EM structure of the human SSU processome, state post-A1 · an experimental structure of the same protein · chain A against LJ, TM-score 0.71
- 7RUO · Crystal structure of human UTP15 · an experimental structure of the same protein · chain A against A, TM-score 0.57
- 7RUO · Crystal structure of human UTP15 · an experimental structure of the same protein · chain A against A, TM-score 0.57
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 Q8TED0
- Elsewhere: UniProt Q8TED0 · AlphaFold DB Q8TED0
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