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Arrestin from bovine rod outer segments

Analyse Arrestin from bovine rod outer segments in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1AYR
Type: protein
Length: 1,462 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Arrestin
UniProt: P08168
Pockets: 18 · best druggability 0.72

Structure

x-ray diffraction · 2 distinct chains · 5% helix, 49% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	Arrestin	protein	368	5% helix, 48% strand	P08168
B, D	Arrestin	protein	363	5% helix, 50% strand	P08168

Pockets

18 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	868	0.72	0.77	75	empty
2	530	0.69	0.79	57	empty
3	50	0.68	0.97	23	empty
4	214	0.61	0.81	34	empty
5	108	0.57	0.85	22	empty

Interfaces

4 interfaces between chains.

B–C · 705 Å² buried · 13 hydrogen bonds · protein-protein
A–D · 681 Å² buried · 10 hydrogen bonds · protein-protein
A–B · 638 Å² buried · 5 hydrogen bonds · protein-protein
C–D · 618 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

1AYR · Arrestin from bovine rod outer segments · the same entry in another collection · chain A against A, TM-score 1.00
P08168 · AlphaFold monomer V2.0 prediction for S-arrestin (P08168) · a predicted model of the same protein · chain A against A, TM-score 0.91

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 P08168
Elsewhere: RCSB PDB 1AYR · PDBe 1AYR · UniProt P08168

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