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Navab voltage-gated sodium channel, residues 1-239 with mutation T206A

Analyse Navab voltage-gated sodium channel, residues 1-239 with mutation T206A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6MWB
Type: protein
Length: 238 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ion transport protein
UniProt: A8EVM5
Ligands: PX4, CPS, SO4
Pockets: 2 · best druggability 0.48

Structure

x-ray diffraction · 1 distinct chain · 86% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Ion transport protein	protein	238	86% helix, 0% strand	A8EVM5

Ligands and binding sites

PX4 · 1,2-dimyristoyl-sn-glycero-3-phosphocholine · ligand · 4 copies · chains B
CPS · 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate · ligand · 2 copies · chains B
SO4 · Sulfate ion · ion · chains B

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	121	0.48	0.80	19	empty
2	71	0.30	0.74	13	empty

Compared structures

6MWB · NavAb Voltage-gated Sodium Channel, residues 1-239 with mutation T206A · the same entry in another collection · chain B against B, 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 6MWB · PDBe 6MWB · UniProt A8EVM5

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