MolNFT v1 · #176779 · protein

Structure of TRPC3 gain of function mutation R803C at 3.2 ångström in 1340NM free calcium state

7DXE: “Structure of TRPC3 gain of function mutation R803C at 3.2 ångström in 1340NM free calcium state”. Electron microscopy, 4 ligands (Y01, POV, 98R). MolNFT v1 #176779 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7DXE
Type: protein
Length: 2,740 residues
Chains: 4
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q13507
Ligands: Y01, POV, 98R, ZN

Structure

electron microscopy · 1 distinct chain.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
D, A, B, C	—	protein	685	—	Q13507

Ligands and binding sites

Y01 · Cholesterol hemisuccinate · ligand · 8 copies · chains D, A, C, B
POV · (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate · ligand · 4 copies · chains D, B, A, C
98R · [(2S)-2-[(E)-octadec-10-enoyl]oxy-3-oxidanyl-propyl] octadec-10-enoate · ligand · 4 copies · chains D, B, A, C
ZN · Zinc ion · metal · 4 copies · chains D, A, B, C

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

Compared structures

7DXE · Structure of TRPC3 gain of function mutation R803C at 3.2 angstrom in 1340nM free calcium… · the same entry in another collection · chain D against D, 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 D against A, TM-score 0.98

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 Q13507
Elsewhere: RCSB PDB 7DXE · PDBe 7DXE · UniProt Q13507

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.