Research workbench
Crystal structure of the C-terminal WD40 domain of TUP1
Analyse Crystal structure of the C-terminal WD40 domain of TUP1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ERJ
- Type
- protein
- Length
- 1,055 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcriptional repressor TUP1
- UniProt
- P16649
- Pockets
- 5 · best druggability 0.82
Structure
x-ray diffraction · 3 distinct chains · 3% helix, 51% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcriptional repressor TUP1 | protein | 350 | 2% helix, 51% strand | P16649 |
| B | Transcriptional repressor TUP1 | protein | 348 | 4% helix, 51% strand | P16649 |
| C | Transcriptional repressor TUP1 | protein | 357 | 3% helix, 50% strand | P16649 |
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 685 | 0.82 | 0.86 | 54 | empty |
| 2 | 623 | 0.81 | 0.86 | 49 | empty |
| 3 | 704 | 0.81 | 0.85 | 62 | empty |
| 4 | 320 | 0.58 | 0.77 | 36 | empty |
| 5 | 234 | 0.49 | 0.74 | 28 | empty |
Interfaces
3 interfaces between chains.
- A–B · 200 Ų buried · 1 hydrogen bond · protein-protein
- B–C · 149 Ų buried · 0 hydrogen bonds · protein-protein
- A–C · 109 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 1ERJ · Crystal structure of the C-terminal WD40 domain of TUP1 · the same entry in another collection · chain A against A, TM-score 1.00
- P16649 · AlphaFold monomer V2.0 prediction for general transcriptional corepressor TUP1 (P16649) · a predicted model of the same protein · chain B against A, TM-score 1.00
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 P16649
- Elsewhere: RCSB PDB 1ERJ · PDBe 1ERJ · UniProt P16649
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