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Full length ARRESTIN2

Analyse Full length ARRESTIN2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2WTR
Type: protein
Length: 723 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-arrestin-1
UniProt: P17870
Ligands: BA
Pockets: 10 · best druggability 0.68

Structure

x-ray diffraction · 2 distinct chains · 4% helix, 45% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-arrestin-1	protein	356	5% helix, 46% strand	P17870
B	Beta-arrestin-1	protein	367	3% helix, 44% strand	P17870

Ligands and binding sites

BA · Barium ion · metal · 4 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	52	0.68	0.97	15	empty
2	742	0.67	0.75	81	empty
3	83	0.64	0.91	24	empty
4	336	0.59	0.77	46	empty
5	69	0.48	0.83	22	empty

Interfaces

1 interface between chains.

A–B · 425 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

2WTR · Full length Arrestin2 · the same entry in another collection · chain A against A, TM-score 1.00
P17870 · AlphaFold monomer V2.0 prediction for beta-arrestin-1 (P17870) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 P17870
Elsewhere: RCSB PDB 2WTR · PDBe 2WTR · UniProt P17870

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