GL1X · GenesisL1 explorer

Research workbench

Crystal structure of N2C/D282C stabilized opsin bound to RS16

Analyse Crystal structure of N2C/D282C stabilized opsin bound to RS16 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6FKD
Type
protein
Length
326 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Rhodopsin
UniProt
P02699
Ligands
ACE, PLM, DL2, NAG, MAN, BMA
Pockets
4 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 69% helix, 4% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARhodopsinprotein32669% helix, 4% strandP02699

Ligands and binding sites

  • ACE · Acetyl group · ligand · chains A
  • PLM · Palmitic acid · ligand · chains A
  • DL2 · 5-chloranyl-2-(2-oxidanylidene-2-spiro[1,3-benzodioxole-2,4'-piperidine]-1'-yl-ethyl)-3~{H}-pyridin-6-one · ligand · chains A
  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
  • MAN · alpha-D-mannopyranose · sugar · 2 copies
  • BMA · beta-D-mannopyranose · sugar
  • BOG · octyl beta-D-glucopyranoside · additive · 5 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, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17090.830.8668BOG, DL2
21130.570.8423BOG
32150.490.7523empty
4530.300.7511empty

Modifications

Observed in the structure: 2 covalent, 2 disulfide, 1 glycan, 1 lipid (disulfide, additive adduct, covalent ligand, N-glycosylation, palmitoylation).

Compared structures

  • 6FKD · Crystal structure of N2C/D282C stabilized opsin bound to RS16 · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.