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Crystal structure of bovine opsin with nerol bound

Analyse Crystal structure of bovine opsin with nerol bound in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6PH7
Type
protein
Length
337 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Rhodopsin; G protein CT2 peptide
UniProt
P02699
Ligands
PLM, NZZ, NAG, BMA
Pockets
3 · best druggability 0.84

Structure

x-ray diffraction · 2 distinct chains · 71% helix, 4% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARhodopsinprotein32671% helix, 4% strandP02699
BG protein CT2 peptideprotein1155% helix, 0% strand—

Ligands and binding sites

  • PLM · Palmitic acid · ligand · chains A
  • NZZ · (2Z)-3,7-dimethylocta-2,6-dien-1-ol · ligand · chains A
  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
  • BMA · beta-D-mannopyranose · sugar · 2 copies
  • BOG · octyl beta-D-glucopyranoside · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12970.840.9435NZZ
21290.530.8120empty
3680.320.7514empty

Interfaces

1 interface between chains.

  • A–B · 675 Ų buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide, 1 glycan, 1 lipid (disulfide, N-glycosylation, palmitoylation).

Compared structures

  • 6PH7 · Crystal structure of bovine opsin with nerol bound · the same entry in another collection · chain A against A, TM-score 1.00

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