Research workbench
Cryo-EM structure of the saga and NUA4 coactivator subunit TRA1
Analyse Cryo-EM structure of the saga and NUA4 coactivator subunit TRA1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5OJS
- Type
- protein
- Length
- 3,473 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcription-associated protein 1
- UniProt
- P38811
- Pockets
- 20 · best druggability 0.85
Structure
electron microscopy · 1 distinct chain · 55% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| T | Transcription-associated protein 1 | protein | 3473 | 55% helix, 1% strand | P38811 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1083 | 0.85 | 0.86 | 101 | empty |
| 2 | 928 | 0.85 | 0.86 | 91 | empty |
| 3 | 1093 | 0.83 | 0.84 | 107 | empty |
| 4 | 953 | 0.81 | 0.82 | 114 | empty |
| 5 | 846 | 0.76 | 0.80 | 90 | 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 P38811
- Elsewhere: RCSB PDB 5OJS · PDBe 5OJS · UniProt P38811
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