Research workbench
Hexagonal crystal structure of TAS3 C-terminal alpha motif
Analyse Hexagonal crystal structure of TAS3 C-terminal alpha motif in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3D1D
- Type
- protein
- Length
- 654 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RNA-induced transcriptional silencing complex protein TAS3
- UniProt
- O94687
- Pockets
- 6 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 74% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | RNA-induced transcriptional silencing complex protein TAS3 | protein | 109 | 74% helix, 2% strand | O94687 |
Pockets
6 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1180 | 0.79 | 0.81 | 86 | empty |
| 2 | 58 | 0.68 | 0.96 | 17 | empty |
| 3 | 286 | 0.61 | 0.79 | 32 | empty |
| 4 | 290 | 0.59 | 0.78 | 36 | empty |
| 5 | 194 | 0.54 | 0.79 | 26 | empty |
Interfaces
8 interfaces between chains.
- A–B · 723 Ų buried · 6 hydrogen bonds · protein-protein
- C–D · 706 Ų buried · 6 hydrogen bonds · protein-protein
- E–F · 576 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 558 Ų buried · 7 hydrogen bonds · protein-protein
- B–D · 480 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 3D1D · Hexagonal crystal structure of Tas3 C-terminal alpha motif · the same entry in another collection · chain E against E, TM-score 1.00
- O94687 · AlphaFold monomer V2.0 prediction for RNA-induced transcriptional silencing complex… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 O94687
- Elsewhere: RCSB PDB 3D1D · PDBe 3D1D · UniProt O94687
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