Research workbench
Structure of the human SRP68-RBD
Analyse Structure of the human SRP68-RBD in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4P3F
- Type
- protein
- Length
- 391 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.699
- Source
- Homo sapiens
- Molecule
- Signal recognition particle subunit SRP68
- UniProt
- Q9UHB9
- Pockets
- 3 · best druggability 0.80
Structure
x-ray diffraction · resolution 1.699 · 2 distinct chains · 76% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Signal recognition particle subunit SRP68 | protein | 193 | 76% helix, 1% strand | Q9UHB9 |
| B | Signal recognition particle subunit SRP68 | protein | 198 | 76% helix, 2% strand | Q9UHB9 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 4 copies · chains A
- PEG · Di(hydroxyethyl)ether · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 667 | 0.80 | 0.85 | 63 | empty |
| 2 | 250 | 0.67 | 0.84 | 34 | empty |
| 3 | 75 | 0.32 | 0.74 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 899 Ų buried · 13 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 Q9UHB9
- Elsewhere: RCSB PDB 4P3F · PDBe 4P3F · UniProt Q9UHB9
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