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Anomalous bromide substructure of nmhr under continuous illumination determined at 13.7 kev with serial crystallography
Analyse Anomalous bromide substructure of nmhr under continuous illumination determined… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7O8Z
- Type
- protein
- Length
- 262 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chloride pumping rhodopsin
- UniProt
- W8VZW3
- Ligands
- OLA, RET, BR
- Pockets
- 1 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 82% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chloride pumping rhodopsin | protein | 262 | 82% helix, 3% strand | W8VZW3 |
Ligands and binding sites
- OLA · Oleic acid · ligand · 6 copies · chains A
- RET · Retinal · ligand · chains A
- BR · Bromide ion · ion · 9 copies · chains A
- OLC · (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate · additive · 2 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 | 138 | 0.73 | 0.91 | 23 | RET |
Modifications
Observed in the structure: 1 cofactor (retinal Schiff base).
Compared structures
- 7O8Z · Anomalous bromide substructure of NmHR under continuous illumination determined at 13.7… · 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 W8VZW3
- Elsewhere: RCSB PDB 7O8Z · PDBe 7O8Z · UniProt W8VZW3
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