Research workbench
X-ray structure of bacteriorhodopsin grown in lipidic cubic phases
Analyse X-ray structure of bacteriorhodopsin grown in lipidic cubic phases in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1QHJ
- Type
- protein
- Length
- 228 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (bacteriorhodopsin)
- UniProt
- P02945
- Ligands
- PH1, RET
- Pockets
- 1 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 76% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (bacteriorhodopsin) | protein | 228 | 76% helix, 5% strand | P02945 |
Ligands and binding sites
- PH1 · 1,2-[di-2,6,10,14-tetramethyl-hexadecan-16-oxy]-propane · ligand · 9 copies · chains A
- RET · Retinal · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 118 | 0.79 | 0.98 | 26 | RET |
Modifications
Observed in the structure: 1 cofactor (retinal Schiff base).
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 P02945
- Elsewhere: RCSB PDB 1QHJ · PDBe 1QHJ · UniProt P02945
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