Research workbench
Crystal structure of the natural light-gated anion channel GTACR1
Analyse Crystal structure of the natural light-gated anion channel GTACR1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6CSM
- Type
- protein
- Length
- 1,092 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GTACR1
- UniProt
- L1J207
- Ligands
- OLA, RET
- Pockets
- 15 · best druggability 0.87
Structure
x-ray diffraction · 3 distinct chains · 66% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GTACR1 | protein | 275 | 66% helix, 4% strand | L1J207 |
| B, C | GTACR1 | protein | 270 | 67% helix, 5% strand | L1J207 |
| D | GTACR1 | protein | 277 | 65% helix, 5% strand | L1J207 |
Ligands and binding sites
- OLA · Oleic acid · ligand · 5 copies · chains A, B, C, D
- RET · Retinal · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1111 | 0.87 | 0.88 | 105 | RET |
| 2 | 174 | 0.77 | 0.93 | 25 | RET |
| 3 | 190 | 0.75 | 0.91 | 27 | RET |
| 4 | 727 | 0.71 | 0.77 | 68 | empty |
| 5 | 54 | 0.70 | 0.98 | 21 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1404 Ų buried · 7 hydrogen bonds · protein-protein
- C–D · 1358 Ų buried · 6 hydrogen bonds · protein-protein
- B–C · 660 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide, 4 cofactor (disulfide, retinal Schiff base).
Compared structures
- 6CSM · Crystal structure of the natural light-gated anion channel 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 6CSM · PDBe 6CSM · UniProt L1J207
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