Research workbench

Crystal structure of C-terminally truncated arrestin reveals mechanism of arrestin activation

Analyse Crystal structure of C-terminally truncated arrestin reveals mechanism of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4J2Q
Type: protein
Length: 686 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: S-arrestin
UniProt: P08168
Pockets: 9 · best druggability 0.71

Structure

x-ray diffraction · 2 distinct chains · 3% helix, 51% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	S-arrestin	protein	340	4% helix, 52% strand	P08168
B	S-arrestin	protein	346	3% helix, 50% strand	P08168

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	780	0.71	0.77	66	empty
2	447	0.60	0.75	40	empty
3	184	0.50	0.77	25	empty
4	205	0.49	0.76	32	empty
5	63	0.40	0.81	20	empty

Interfaces

1 interface between chains.

A–B · 1113 Å² buried · 22 hydrogen bonds · protein-protein

Compared structures

4J2Q · Crystal structure of C-terminally truncated arrestin reveals mechanism of arrestin… · 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 0.90

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 4J2Q · PDBe 4J2Q · UniProt P08168

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