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BETA3 subunit of voltage-gated CA2+-channel

Analyse BETA3 subunit of voltage-gated CA2+-channel in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1VYU
Type: protein
Length: 557 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Calcium channel beta-3 subunit
UniProt: P54287
Pockets: 3 · best druggability 0.69

Structure

x-ray diffraction · 2 distinct chains · 43% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Calcium channel beta-3 subunit	protein	271	43% helix, 20% strand	P54287
B	Calcium channel beta-3 subunit	protein	286	43% helix, 19% strand	P54287

Pockets

3 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	440	0.69	0.80	53	empty
2	206	0.50	0.76	34	empty
3	165	0.44	0.75	24	empty

Interfaces

1 interface between chains.

A–B · 950 Å² buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 modified (engineered).

Compared structures

1VYU · Beta3 subunit of Voltage-gated Ca2+-channel · the same entry in another collection · chain A against A, TM-score 1.00
P54287 · AlphaFold monomer V2.0 prediction for voltage-dependent L-type calcium channel subunit… · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P54287
Elsewhere: RCSB PDB 1VYU · PDBe 1VYU · UniProt P54287

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