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Crystal of ARRESTIN2-V2RPP-4-FAB30 complex

Analyse Crystal of ARRESTIN2-V2RPP-4-FAB30 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7DFA
Type: protein
Length: 812 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-arrestin-1; FAB30 heavy chain; FAB30 light chain; Varpp-4
UniProt: P17870
Pockets: 13 · best druggability 0.79

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-arrestin-1	protein	363	4% helix, 46% strand	P17870
H	FAB30 heavy chain	protein	216	3% helix, 48% strand	—
L	FAB30 light chain	protein	210	6% helix, 46% strand	—
V	Varpp-4	protein	23	0% helix, 30% strand	—

Pockets

13 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	374	0.79	0.88	52	empty
2	713	0.76	0.81	65	empty
3	119	0.58	0.85	35	empty
4	326	0.58	0.77	49	empty
5	368	0.55	0.74	49	empty

Interfaces

5 interfaces between chains.

H–L · 1693 Å² buried · 13 hydrogen bonds · protein-protein
A–V · 1213 Å² buried · 30 hydrogen bonds · protein-protein
A–H · 677 Å² buried · 7 hydrogen bonds · protein-protein
A–L · 327 Å² buried · 6 hydrogen bonds · protein-protein
L–V · 105 Å² buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 7 modified, 4 disulfide (phosphorylation, disulfide).

Compared structures

7DFA · Crystal of Arrestin2-V2Rpp-4-Fab30 complex · the same entry in another collection · chain V against V, 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 0.81

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 7DFA · PDBe 7DFA · UniProt P17870

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