Research workbench
Time-resolved serial femtosecond crystallography reveals early structural changes in channelrhodopsin: 1 ms structure
Analyse Time-resolved serial femtosecond crystallography reveals early structural… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7E71
- Type
- protein
- Length
- 296 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Archaeal-type opsin 1,ARCHAEAL-type opsin 2
- UniProt
- Q93WP2, Q8RUT8
- Ligands
- RET, NAG
- Pockets
- 4 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 62% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Archaeal-type opsin 1,ARCHAEAL-type opsin 2 | protein | 296 | 62% helix, 4% strand | Q93WP2, Q8RUT8 |
Ligands and binding sites
- RET · Retinal · ligand · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
- OLC · (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate · additive · 9 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 240 | 0.81 | 0.93 | 33 | RET |
| 2 | 70 | 0.70 | 0.96 | 24 | empty |
| 3 | 188 | 0.56 | 0.80 | 23 | empty |
| 4 | 87 | 0.37 | 0.77 | 18 | empty |
Modifications
Observed in the structure: 1 cofactor, 1 glycan (retinal Schiff base, N-glycosylation).
Compared structures
- 7E71 · Time-resolved serial femtosecond crystallography reveals early structural changes in… · 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 Q93WP2
- Every structure of UniProt Q8RUT8
- Elsewhere: RCSB PDB 7E71 · PDBe 7E71 · UniProt Q93WP2 · UniProt Q8RUT8
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