Research workbench
AlphaFold monomer V2.0 prediction for T-complex protein 1 subunit delta (Q2T9X2)
Analyse AlphaFold monomer V2.0 prediction for T-complex protein 1 subunit delta (Q2T9X2) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q2T9X2
- Type
- protein
- Length
- 542 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xdc97e953B1a926A79e803518D45128CFF95817d1
- Molecule
- T-complex protein 1 subunit delta
- UniProt
- Q2T9X2
- Pockets
- 3 · best druggability 0.80
Structure
1 distinct chain · 49% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | T-complex protein 1 subunit delta | protein | 542 | 49% helix, 17% strand | Q2T9X2 |
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 | 285 | 0.80 | 0.91 | 42 | empty |
| 2 | 164 | 0.42 | 0.74 | 25 | empty |
| 3 | 70 | 0.33 | 0.76 | 19 | empty |
Compared structures
- 3IYG · Ca model of bovine TRiC/CCT derived from a 4.0 Angstrom cryo-EM map · an experimental structure of the same protein · chain A against D, TM-score 0.85
- 3IYG · Ca model of bovine TRIC/CCT derived from a 4.0 ångström cryo-EM MAP · an experimental structure of the same protein · chain A against D, TM-score 0.85
- 4B2T · The crystal structures of the eukaryotic chaperonin cct reveal its functional partitioning · an experimental structure of the same protein · chain A against D, TM-score 0.74
- 4B2T · The crystal structures of the eukaryotic chaperonin CCT reveal its functional partitioning · an experimental structure of the same protein · chain A against D, TM-score 0.74
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 Q2T9X2
- Elsewhere: UniProt Q2T9X2 · AlphaFold DB Q2T9X2
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