MolNFT v2 · #208899 · protein

Cryo-EM structure of cGMP bound human CNGA3/CNGB3 channel in GDN, transition state 1

8EU3: “Cryo-EM structure of cGMP bound human CNGA3/CNGB3 channel in GDN, transition state 1”. Electron microscopy at 3.62, 2 ligands (PCG, NAG). MolNFT v2 #208899 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 8EU3
Type: protein
Length: 1,770 residues
Chains: 4
Method: electron microscopy
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 3.62
Source: Homo sapiens
UniProt: Q16281, Q9NQW8
Ligands: PCG, NAG

Structure

electron microscopy · resolution 3.62 · 4 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	444	—	Q16281
B	—	protein	443	—	Q16281
C	—	protein	445	—	Q16281
D	—	protein	438	—	Q9NQW8

Ligands and binding sites

PCG · Cyclic guanosine monophosphate · ligand · 4 copies · chains A, B, C, D
NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A, B, C

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

Compared structures

Q16281 · AlphaFold monomer V2.0 prediction for cyclic nucleotide-gated cation channel alpha-3… · a predicted model of the same protein · chain B against A, TM-score 0.96
Q9NQW8 · AlphaFold monomer V2.0 prediction for cyclic nucleotide-gated cation channel beta-3… · a predicted model of the same protein · chain D against A, TM-score 0.94

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 Q16281
Every structure of UniProt Q9NQW8
Elsewhere: RCSB PDB 8EU3 · PDBe 8EU3 · UniProt Q16281 · UniProt Q9NQW8

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