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MolNFT v1 · #189990 · protein

Cryo-EM structure of human NAV1.7(E406K)-BETA1-BETA2 complex

7W9L: “Cryo-EM structure of human NAV1.7(E406K)-BETA1-BETA2 complex”. Electron microscopy, 6 ligands (LPE, Y01, PCW). MolNFT v1 #189990 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB
7W9L
Type
protein
Length
1,714 residues
Chains
3
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt
Q15858, Q07699, O60939
Ligands
LPE, Y01, PCW, 9Z9, P5S, NAG

Structure

electron microscopy · 3 distinct chains.

ChainMoleculeTypeResiduesSecondary structureUniProt
A—protein1422—Q15858
B—protein173—Q07699
C—protein119—O60939

Ligands and binding sites

  • LPE · 1-O-octadecyl-sn-glycero-3-phosphocholine · ligand · 14 copies · chains A, B
  • Y01 · Cholesterol hemisuccinate · ligand · 6 copies · chains A
  • PCW · 1,2-dioleoyl-sn-glycero-3-phosphocholine · ligand · 5 copies · chains A
  • 9Z9 · (3beta,14beta,17beta,25R)-3-[4-methoxy-3-(methoxymethyl)butoxy]spirost-5-en · ligand · chains A
  • P5S · O-[(R)-{[(2R)-2,3-bis(octadecanoyloxy) propyl]oxy}(hydroxy)phosphoryl]-L-serine · ligand · chains A
  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 11 copies · chains A, B

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

Compared structures

  • 7W9L · Cryo-EM structure of human Nav1.7(E406K)-beta1-beta2 complex · the same entry in another collection · chain B against B, TM-score 1.00
  • O60939 · AlphaFold monomer V2.0 prediction for sodium channel subunit beta-2 (O60939) · a predicted model of the same protein · chain C against A, TM-score 0.99
  • Q07699 · AlphaFold monomer V2.0 prediction for sodium channel subunit beta-1 (Q07699) · a predicted model of the same protein · chain B against A, TM-score 0.93
  • Q15858 · AlphaFold monomer V2.0 prediction for sodium channel protein type 9 subunit alpha (Q15858) · a predicted model of the same protein · chain A against A, TM-score 0.92

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