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Crystal structure of the voltage-gated sodium channel navms (F208L) in complex with endoxifen (2.6 ångström resolution)

Analyse Crystal structure of the voltage-gated sodium channel navms (F208L) in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6SXE
Type: protein
Length: 271 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ion transport protein
UniProt: A0L5S6
Ligands: 2CV, 9XY, 7PG, NA
Pockets: 2 · best druggability 0.48

Structure

x-ray diffraction · 1 distinct chain · 77% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ion transport protein	protein	271	77% helix, 0% strand	A0L5S6

Ligands and binding sites

2CV · Hega-10 · ligand · 2 copies · chains A
9XY · Endoxifen · ligand · 2 copies · chains A
7PG · 2,5,8,11,14,17,20,23-octaoxapentacosan-25-ol · ligand · chains A
NA · Sodium ion · metal · 3 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	143	0.48	0.78	20	empty
2	65	0.36	0.78	15	empty

Compared structures

6SXE · Crystal Structure of the Voltage-Gated Sodium Channel NavMs (F208L) in complex with… · the same entry in another collection · chain A against A, TM-score 1.00

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Every structure of UniProt A0L5S6
Elsewhere: RCSB PDB 6SXE · PDBe 6SXE · UniProt A0L5S6

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