Research workbench
AlphaFold monomer V2.0 prediction for T-complex protein 1 subunit delta (Q54CL2)
Analyse AlphaFold monomer V2.0 prediction for T-complex protein 1 subunit delta (Q54CL2) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q54CL2
- Type
- protein
- Length
- 533 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5e58272ea25a05e06901A2eAe9f63939b344e0c6
- Molecule
- T-complex protein 1 subunit delta
- UniProt
- Q54CL2
- Pockets
- 3 · best druggability 0.80
Structure
1 distinct chain · 50% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | T-complex protein 1 subunit delta | protein | 533 | 50% helix, 17% strand | Q54CL2 |
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 | 339 | 0.80 | 0.90 | 57 | empty |
| 2 | 140 | 0.39 | 0.73 | 26 | empty |
| 3 | 64 | 0.29 | 0.74 | 15 | 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 Q54CL2
- Elsewhere: UniProt Q54CL2 · AlphaFold DB Q54CL2
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