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Crystal structure of bos taurus opsin at 2.7 ångström

Analyse Crystal structure of bos taurus opsin at 2.7 ångström in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5TE3
Type
protein
Length
326 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Rhodopsin
UniProt
P02699
Ligands
PLM, NAG, BMA, MAN, SO4
Pockets
5 · best druggability 0.84

Structure

x-ray diffraction · 1 distinct chain · 70% helix, 4% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARhodopsinprotein32670% helix, 4% strandP02699

Ligands and binding sites

  • PLM · Palmitic acid · ligand · 2 copies · chains A
  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
  • BMA · beta-D-mannopyranose · sugar
  • MAN · alpha-D-mannopyranose · sugar
  • SO4 · Sulfate ion · ion · 2 copies · chains A
  • BOG · octyl beta-D-glucopyranoside · additive · 3 copies · chains A

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

Pockets

5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12740.840.9537BOG
22610.580.7827empty
3680.530.8717empty
41030.510.8219empty
5510.450.8420empty

Modifications

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

Compared structures

  • 5TE3 · Crystal structure of Bos taurus opsin at 2.7 Angstrom · the same entry in another collection · chain A against A, TM-score 1.00
  • P02699 · AlphaFold monomer V2.0 prediction for rhodopsin (P02699) · a predicted model of the same protein · chain A against A, TM-score 0.98

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