Research workbench
Crystal structure of bacteriorhodopsin at pH 10
Analyse Crystal structure of bacteriorhodopsin at pH 10 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1X0K
- Type
- protein
- Length
- 227 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bacteriorhodopsin
- UniProt
- P02945
- Ligands
- L3P, RET, L2P, GLC, MAN, GAL
- Pockets
- 1 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 77% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| 1 | Bacteriorhodopsin | protein | 227 | 77% helix, 5% strand | P02945 |
Ligands and binding sites
- L3P · 2,3-di-O-phytanly-3-sn-glycero-1-phosphoryl-3'-sn-glycerol-1'-phosphate · ligand · 4 copies · chains 1
- RET · Retinal · ligand · chains 1
- L2P · 2,3-di-phytanyl-glycerol · ligand · chains 1
- GLC · alpha-D-glucopyranose · sugar · chains 1
- MAN · alpha-D-mannopyranose · sugar · chains 1
- GAL · beta-D-galactopyranose · sugar
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 | 131 | 0.80 | 0.97 | 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 1X0K · PDBe 1X0K · UniProt P02945
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