MolNFT v1 · #157362 · protein

Navab voltage-gated sodium channel, residues 1-239, with mutation T206V

6MWG · Ion transport protein: “Navab voltage-gated sodium channel, residues 1-239, with mutation T206V”. X-ray diffraction, 2 ligands (PX4, CPS), 2 pockets (best druggability 0.51). MolNFT v1 #157362 on GenesisL1: 3D structure, binding…

PDB: 6MWG
Type: protein
Length: 237 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ion transport protein
UniProt: A8EVM5
Ligands: PX4, CPS
Pockets: 2 · best druggability 0.51

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Ion transport protein	protein	237	85% 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
ACT · Acetate ion · additive · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	123	0.51	0.81	20	empty
2	51	0.24	0.73	12	empty

Compared structures

6MWG · NavAb Voltage-gated Sodium Channel, residues 1-239, with mutation T206V · 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 6MWG · PDBe 6MWG · UniProt A8EVM5

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