Research workbench
Structure of grlr-lipid complex
Analyse Structure of grlr-lipid complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3E3C
- Type
- protein
- Length
- 236 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- L0044
- UniProt
- O85638
- Ligands
- HHG
- Pockets
- 2 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 3% helix, 59% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | L0044 | protein | 118 | 3% helix, 59% strand | O85638 |
Ligands and binding sites
- HHG · (2R)-2-hydroxy-3-(phosphonooxy)propyl hexanoate · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 243 | 0.78 | 0.91 | 43 | HHG |
| 2 | 186 | 0.77 | 0.92 | 36 | HHG |
Interfaces
1 interface between chains.
- A–B · 995 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 3E3C · Structure of GrlR-lipid complex · the same entry in another collection · chain A 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 O85638
- Elsewhere: RCSB PDB 3E3C · PDBe 3E3C · UniProt O85638
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