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MolNFT v1 · #145652 · protein

Structure of the human TRPC3 in a lipid-occupied, closed state

6CUD: “Structure of the human TRPC3 in a lipid-occupied, closed state”. Electron microscopy, 3 ligands (6OE, FGJ, NAG). MolNFT v1 #145652 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB
6CUD
Type
protein
Length
2,816 residues
Chains
4
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt
Q13507
Ligands
6OE, FGJ, NAG

Structure

electron microscopy · 1 distinct chain.

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D—protein704—Q13507

Ligands and binding sites

  • 6OE · (2S)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(hexanoyloxy)propyl hexanoate · ligand · 4 copies · chains A, B, C, D
  • FGJ · (2R)-3-hydroxypropane-1,2-diyl dihexanoate · ligand · 4 copies · chains A, D, B, C
  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A, B, C, D

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

Compared structures

  • 6CUD · Structure of the human TRPC3 in a lipid-occupied, closed state · the same entry in another collection · chain A against A, TM-score 1.00
  • Q13507 · AlphaFold monomer V2.0 prediction for short transient receptor potential channel 3… · a predicted model of the same protein · chain A against A, TM-score 0.95

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