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Navab voltage-gated sodium channel, residues 1-226, crystallized in the presence of class 1B anti-arrhythmic drug lidocaine

Analyse Navab voltage-gated sodium channel, residues 1-226, crystallized in the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6MVY
Type: protein
Length: 446 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ion transport protein
UniProt: A8EVM5
Ligands: PX4, SO4
Pockets: 3 · best druggability 0.49

Structure

x-ray diffraction · 1 distinct chain · 85% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Ion transport protein	protein	223	85% helix, 0% strand	A8EVM5

Ligands and binding sites

PX4 · 1,2-dimyristoyl-sn-glycero-3-phosphocholine · ligand · 8 copies · chains A, B
SO4 · Sulfate ion · ion · 2 copies · chains A, B

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

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	147	0.49	0.78	19	empty
2	134	0.49	0.79	20	empty
3	72	0.30	0.74	17	empty

Compared structures

6MVY · NavAb voltage-gated sodium channel, residues 1-226, crystallized in the presence of Class… · the same entry in another collection · chain A against A, TM-score 1.00

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 A8EVM5
Elsewhere: RCSB PDB 6MVY · PDBe 6MVY · UniProt A8EVM5

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