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MolNFT v1 · #151273 · protein

Mouse serotonin 5-HT3 receptor, serotonin-bound, I2 conformation

6HIQ · 5-hydroxytryptamine receptor 3A: “Mouse serotonin 5-HT3 receptor, serotonin-bound, I2 conformation”. Electron microscopy, 2 ligands (SRO, NAG), 20 pockets (best druggability 0.87). MolNFT v1 #151273 on GenesisL1: 3D structure…

PDB
6HIQ
Type
protein
Length
1,925 residues
Chains
5
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
5-hydroxytryptamine receptor 3A
UniProt
E9QLC0
Ligands
SRO, NAG
Pockets
20 · best druggability 0.87

Structure

electron microscopy · 1 distinct chain · 39% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, E, B, C, D5-hydroxytryptamine receptor 3Aprotein38539% helix, 25% strandE9QLC0

Ligands and binding sites

  • SRO · Serotonin · ligand · 5 copies · chains A, E, D, B, C
  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 25 copies · chains A, E, B, C, D

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

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17900.870.90106empty
27980.860.88103empty
35150.840.9079empty
43580.810.9048empty
57390.800.8472empty

Interfaces

5 interfaces between chains.

  • A–E · 3397 Ų buried · 26 hydrogen bonds · protein-protein
  • A–B · 3333 Ų buried · 24 hydrogen bonds · protein-protein
  • B–C · 3311 Ų buried · 24 hydrogen bonds · protein-protein
  • C–D · 3288 Ų buried · 20 hydrogen bonds · protein-protein
  • E–D · 3225 Ų buried · 19 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 15 glycan, 5 disulfide (N-glycosylation, disulfide).

Compared structures

  • 6HIQ · Mouse serotonin 5-HT3 receptor, serotonin-bound, I2 conformation · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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