MolNFT v1 · #74624 · protein

Crystal structure of arrestin-3 reveals the basis of the difference in receptor binding between two non-visual subtypes

3P2D · Beta-arrestin-2: “Crystal structure of arrestin-3 reveals the basis of the difference in receptor binding between two…”. X-ray diffraction, 13 pockets (best druggability 0.72). MolNFT v1 #74624 on GenesisL1: 3D structure, binding…

PDB: 3P2D
Type: protein
Length: 706 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-arrestin-2
UniProt: P32120
Pockets: 13 · best druggability 0.72

Structure

x-ray diffraction · 2 distinct chains · 4% helix, 46% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-arrestin-2	protein	354	5% helix, 47% strand	P32120
B	Beta-arrestin-2	protein	352	3% helix, 46% strand	P32120

Pockets

13 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	59	0.72	0.98	19	empty
2	99	0.69	0.92	29	empty
3	167	0.54	0.80	25	empty
4	132	0.50	0.80	26	empty
5	52	0.47	0.85	19	empty

Interfaces

1 interface between chains.

A–B · 279 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

3P2D · Crystal structure of arrestin-3 reveals the basis of the difference in receptor binding… · 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 B 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 P32120
Elsewhere: RCSB PDB 3P2D · PDBe 3P2D · UniProt P32120

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