Research workbench
The 97H/F mutant structure of a glutamine-rich domain from histone deacetylase 4
Analyse The 97H/F mutant structure of a glutamine-rich domain from histone deacetylase 4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2O94
- Type
- protein
- Length
- 272 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone deacetylase 4
- UniProt
- P56524
- Pockets
- 4 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 90% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Histone deacetylase 4 | protein | 68 | 90% helix, 0% strand | P56524 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 85 | 0.77 | 0.98 | 18 | empty |
| 2 | 79 | 0.75 | 0.98 | 18 | empty |
| 3 | 76 | 0.34 | 0.75 | 18 | empty |
| 4 | 55 | 0.31 | 0.76 | 12 | empty |
Interfaces
6 interfaces between chains.
- B–D · 1366 Ų buried · 7 hydrogen bonds · protein-protein
- A–C · 1366 Ų buried · 9 hydrogen bonds · protein-protein
- A–D · 850 Ų buried · 7 hydrogen bonds · protein-protein
- B–C · 841 Ų buried · 9 hydrogen bonds · protein-protein
- A–B · 639 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 2O94 · The 97H/F mutant Structure of a glutamine-rich domain from histone deacetylase 4 · the same entry in another collection · chain A against A, TM-score 1.00
- P56524 · AlphaFold monomer V2.0 prediction for histone deacetylase 4 (P56524) · a predicted model of the same protein · chain A against A, TM-score 0.83
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 P56524
- Elsewhere: RCSB PDB 2O94 · PDBe 2O94 · UniProt P56524
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