Research workbench
Ground state structure of archaerhodopsin-3 at 100K
Analyse Ground state structure of archaerhodopsin-3 at 100K in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6S6C
- Type
- protein
- Length
- 241 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Archaerhodopsin-3
- UniProt
- P96787
- Ligands
- R16, RET, D12, CA, NA, CL
- Pockets
- 1 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 74% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Archaerhodopsin-3 | protein | 241 | 74% helix, 5% strand | P96787 |
Ligands and binding sites
- R16 · Hexadecane · ligand · 6 copies · chains A
- RET · Retinal · ligand · chains A
- D12 · Dodecane · ligand · chains A
- CA · Calcium ion · metal · chains A
- NA · Sodium ion · metal · chains A
- CL · Chloride ion · ion · 3 copies · chains A
- DD9 · nonane · additive · 4 copies · chains A
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 | 119 | 0.80 | 0.98 | 26 | RET |
Modifications
Observed in the structure: 1 cofactor, 1 modified (retinal Schiff base, cyclization).
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 P96787
- Elsewhere: RCSB PDB 6S6C · PDBe 6S6C · UniProt P96787
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