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Cryo-EM structure of hDisp1NNN-3C-Cleavage

Analyse Cryo-EM structure of hDisp1NNN-3C-Cleavage in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7E2H
Type
protein
Length
907 residues
Chains
2
Method
electron microscopy
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
3.68
Source
Homo sapiens
Molecule
Protein dispatched homolog 1
UniProt
Q96F81
Ligands
Y01, NAG
Pockets
14 · best druggability 0.73

Structure

electron microscopy · resolution 3.68 · 2 distinct chains · 53% helix, 4% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
DProtein dispatched homolog 1protein8352% helix, 0% strandQ96F81
EProtein dispatched homolog 1protein82453% helix, 5% strandQ96F81

Ligands and binding sites

  • Y01 · Cholesterol hemisuccinate · ligand · 8 copies · chains E, D
  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains E

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

Pockets

14 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12720.730.8641empty
22000.650.8427empty
31500.630.8520empty
41470.620.8528empty
51610.580.8234empty

Interfaces

1 interface between chains.

  • D–E · 3264 Ų buried · 12 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 glycan (N-glycosylation).

Compared structures

  • 7E2H · Cryo-EM structure of HDISP1NNN-3C-cleavage · the same entry in another collection · chain D against D, TM-score 1.00
  • Q96F81 · AlphaFold monomer V2.0 prediction for protein dispatched homolog 1 (Q96F81) · a predicted model of the same protein · chain E against A, TM-score 0.93

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