Research workbench
Structure of DOS1 propeller
Analyse Structure of DOS1 propeller in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4O9D
- Type
- protein
- Length
- 783 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RIK1-associated factor 1
- UniProt
- O74910
- Ligands
- CL
- Pockets
- 4 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 3% helix, 51% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | RIK1-associated factor 1 | protein | 392 | 2% helix, 50% strand | O74910 |
| A | RIK1-associated factor 1 | protein | 391 | 4% helix, 52% strand | O74910 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1128 | 0.78 | 0.80 | 69 | empty |
| 2 | 1129 | 0.77 | 0.79 | 73 | EDO |
| 3 | 686 | 0.65 | 0.74 | 57 | EDO |
| 4 | 137 | 0.44 | 0.76 | 17 | empty |
Interfaces
1 interface between chains.
- B–A · 411 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
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 O74910
- Elsewhere: RCSB PDB 4O9D · PDBe 4O9D · UniProt O74910
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