Research workbench
Crystal structure of thermoplasmatales archaeon heliorhodopsin
Analyse Crystal structure of thermoplasmatales archaeon heliorhodopsin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6IS6
- Type
- protein
- Length
- 250 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Heliorhodopsin
- UniProt
- A0A151EDA9
- Ligands
- RET
- Pockets
- 1 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 73% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Heliorhodopsin | protein | 250 | 73% helix, 8% strand | A0A151EDA9 |
Ligands and binding sites
- RET · Retinal · ligand · chains A
- OLC · (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate · additive · 14 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 | 191 | 0.75 | 0.90 | 29 | OLC, RET |
Modifications
Observed in the structure: 1 cofactor (retinal Schiff base).
Compared structures
- 6IS6 · Crystal structure of Thermoplasmatales archaeon heliorhodopsin · 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 A0A151EDA9
- Elsewhere: RCSB PDB 6IS6 · PDBe 6IS6 · UniProt A0A151EDA9
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