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

Analyse Mouse serotonin 5-HT3 receptor, serotonin-bound, F conformation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6HIN
Type
protein
Length
1,675 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
17 · best druggability 0.82

Structure

electron microscopy · 1 distinct chain · 32% helix, 27% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E5-hydroxytryptamine receptor 3Aprotein33532% helix, 27% strandE9QLC0

Ligands and binding sites

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

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

Pockets

17 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15810.820.8796SRO
210280.810.8297empty
35450.810.8787SRO
45200.800.8681SRO
54860.780.8675SRO

Interfaces

5 interfaces between chains.

  • A–E · 2897 Ų buried · 15 hydrogen bonds · protein-protein
  • D–E · 2894 Ų buried · 13 hydrogen bonds · protein-protein
  • C–D · 2889 Ų buried · 15 hydrogen bonds · protein-protein
  • B–C · 2887 Ų buried · 14 hydrogen bonds · protein-protein
  • A–B · 2874 Ų buried · 14 hydrogen bonds · protein-protein

Modifications

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

Compared structures

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

Analyse

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