Research workbench

Active arrestin-3 with inositol hexakisphosphate

Analyse Active arrestin-3 with inositol hexakisphosphate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5TV1
Type: protein
Length: 337 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-arrestin-2
UniProt: P32120
Ligands: IHP
Pockets: 6 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 7% helix, 50% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-arrestin-2	protein	337	7% helix, 50% strand	P32120

Ligands and binding sites

IHP · Inositol hexakisphosphate · ligand · 2 copies · chains A
GOL · Glycerol · additive · 3 copies · chains A

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

Pockets

6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	155	0.51	0.79	26	empty
2	194	0.50	0.77	31	empty
3	115	0.47	0.79	19	empty
4	57	0.35	0.78	17	empty
5	66	0.27	0.72	22	empty

Compared structures

5TV1 · active arrestin-3 with inositol hexakisphosphate · the same entry in another collection · chain A against A, TM-score 1.00
P32120 · AlphaFold monomer V2.0 prediction for beta-arrestin-2 (P32120) · a predicted model of the same protein · chain A against A, TM-score 0.94

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 P32120
Elsewhere: RCSB PDB 5TV1 · PDBe 5TV1 · UniProt P32120

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