Research workbench
Crystal structure of N24Q/C128T mutant of channelrhodopsin 2
Analyse Crystal structure of N24Q/C128T mutant of channelrhodopsin 2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6EIG
- Type
- protein
- Length
- 500 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Archaeal-type opsin 2
- UniProt
- Q8RUT8
- Ligands
- LFA, PO4
- Pockets
- 4 · best druggability 0.83
Structure
x-ray diffraction · 2 distinct chains · 73% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Archaeal-type opsin 2 | protein | 250 | 72% helix, 2% strand | Q8RUT8 |
| B | Archaeal-type opsin 2 | protein | 250 | 74% helix, 2% strand | Q8RUT8 |
Ligands and binding sites
- LFA · Eicosane · ligand · 2 copies · chains A
- PO4 · Phosphate ion · ion · 2 copies · chains A, B
- OLC · (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate · additive · 7 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1054 | 0.83 | 0.83 | 76 | OLC |
| 2 | 81 | 0.42 | 0.80 | 16 | empty |
| 3 | 87 | 0.42 | 0.79 | 16 | empty |
| 4 | 50 | 0.29 | 0.76 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 640 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (nonstandard).
Compared structures
- 6EIG · Crystal structure of N24Q/C128T mutant of Channelrhodopsin 2 · 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 Q8RUT8
- Elsewhere: RCSB PDB 6EIG · PDBe 6EIG · UniProt Q8RUT8
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