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Cryo-EM structure of murine dispatched 'T' conformation

Analyse Cryo-EM structure of murine dispatched 'T' conformation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7RPI
Type
protein
Length
926 residues
Chains
1
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein dispatched homolog 1
UniProt
Q3TDN0
Ligands
Y01, AV0, NAG, NA
Pockets
15 · best druggability 0.65

Structure

electron microscopy · 1 distinct chain · 59% helix, 8% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein dispatched homolog 1protein92659% helix, 8% strandQ3TDN0

Ligands and binding sites

  • Y01 · Cholesterol hemisuccinate · ligand · 26 copies · chains A
  • AV0 · 2-decyl-2-{[(4-O-alpha-D-glucopyranosyl-beta-D-glucopyranosyl)oxy]methyl}dodecyl 4-O-alpha-D-glucopyranosyl-beta-D-glucopyranoside · ligand · 2 copies · chains A
  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 5 copies · chains A
  • NA · Sodium ion · metal · 2 copies · chains A

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

Pockets

15 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11920.650.8532empty
21950.630.8323empty
32160.540.7827Y01
41130.540.8321empty
52090.530.7621Y01

Modifications

Observed in the structure: 8 disulfide, 5 glycan (disulfide, N-glycosylation).

Compared structures

  • 7RPI · Cryo-EM structure of murine Dispatched 'T' conformation · the same entry in another collection · chain A against A, TM-score 1.00
  • Q3TDN0 · AlphaFold monomer V2.0 prediction for protein dispatched homolog 1 (Q3TDN0) · a predicted model of the same protein · chain A against A, TM-score 0.97

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