Research workbench
Crystal structure of the light-gated anion channelrhodopsin GTACR1
Analyse Crystal structure of the light-gated anion channelrhodopsin GTACR1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6EDQ
- Type
- protein
- Length
- 542 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Anion channelrhodopsin 1
- UniProt
- L1J207
- Pockets
- 9 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 69% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Anion channelrhodopsin 1 | protein | 267 | 69% helix, 4% strand | L1J207 |
| B | Anion channelrhodopsin 1 | protein | 275 | 69% helix, 4% strand | L1J207 |
Ligands and binding sites
- OLC · (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate · additive · 8 copies · chains A, B
- GOL · Glycerol · additive · 5 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 59 | 0.70 | 0.97 | 18 | empty |
| 2 | 443 | 0.67 | 0.78 | 46 | GOL, OLC |
| 3 | 52 | 0.64 | 0.95 | 20 | empty |
| 4 | 386 | 0.63 | 0.77 | 42 | OLC, GOL |
| 5 | 344 | 0.62 | 0.78 | 31 | empty |
Interfaces
1 interface between chains.
- A–B · 1232 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide, 2 modified (disulfide, nonstandard).
Compared structures
- 6EDQ · Crystal Structure of the Light-Gated Anion Channelrhodopsin GtACR1 · 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 L1J207
- Elsewhere: RCSB PDB 6EDQ · PDBe 6EDQ · UniProt L1J207
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