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Crystal structure of rhodopsin bound to visual arrestin

Analyse Crystal structure of rhodopsin bound to visual arrestin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5DGY
Type
protein
Length
3,128 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
ENDOLYSIN,RHODOPSIN,S-arrestin
EC
3.2.1.17
UniProt
P00720, P08100, P20443
Pockets
20 · best druggability 0.86

Structure

x-ray diffraction · 3 distinct chains · 40% helix, 23% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, DENDOLYSIN,RHODOPSIN,S-arrestin (EC 3.2.1.17)protein83342% helix, 22% strandP00720, P08100, P20443
BENDOLYSIN,RHODOPSIN,S-arrestin (EC 3.2.1.17)protein67336% helix, 25% strandP00720, P08100, P20443
CENDOLYSIN,RHODOPSIN,S-arrestin (EC 3.2.1.17)protein78942% helix, 22% strandP00720, P08100, P20443

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13030.860.9639empty
23110.840.9444empty
32930.830.9344empty
42820.830.9341empty
58920.740.7892empty

Interfaces

3 interfaces between chains.

  • B–D · 522 Ų buried · 2 hydrogen bonds · protein-protein
  • A–C · 464 Ų buried · 1 hydrogen bond · protein-protein
  • B–C · 412 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

  • 5DGY · Crystal structure of rhodopsin bound to visual arrestin · the same entry in another collection · chain C against C, TM-score 1.00
  • P20443 · AlphaFold monomer V2.0 prediction for S-arrestin (P20443) · a predicted model of the same protein · chain B against A, TM-score 0.50
  • P08100 · AlphaFold monomer V2.0 prediction for rhodopsin (P08100) · a predicted model of the same protein · chain B against A, TM-score 0.48

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