Research workbench

Visual arrestin mutant - R175E

Analyse Visual arrestin mutant - R175E in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4ZRG
Type: protein
Length: 343 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: S-arrestin
UniProt: P08168
Ligands: CO2
Pockets: 2 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 6% helix, 50% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	S-arrestin	protein	343	6% helix, 50% strand	P08168

Ligands and binding sites

CO2 · Carbon dioxide · ion · 5 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	159	0.56	0.82	44	CO2
2	51	0.33	0.78	16	empty

Compared structures

4ZRG · Visual arrestin mutant - R175E · 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 0.94

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 P08168
Elsewhere: RCSB PDB 4ZRG · PDBe 4ZRG · UniProt P08168

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