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Crystal structure of human JUNO (crystal form 1)

Analyse Crystal structure of human JUNO (crystal form 1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5JKA
Type
protein
Length
399 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2
Source
Homo sapiens
Molecule
Sperm-egg fusion protein Juno
UniProt
A6ND01
Ligands
NAG, BMA, MAN, CL
Pockets
4 · best druggability 0.62

Structure

x-ray diffraction · resolution 2 · 2 distinct chains · 35% helix, 10% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
BSperm-egg fusion protein Junoprotein19935% helix, 10% strandA6ND01
ASperm-egg fusion protein Junoprotein20035% helix, 10% strandA6ND01

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains B
  • BMA · beta-D-mannopyranose · sugar
  • MAN · alpha-D-mannopyranose · sugar
  • CL · Chloride ion · ion · 3 copies · chains B, A

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

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12440.620.8130empty
22540.610.8032empty
3690.300.7313empty
4710.290.7319empty

Interfaces

1 interface between chains.

  • B–A · 874 Ų buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 16 disulfide, 1 glycan (disulfide, N-glycosylation).

Compared structures

  • 5JKA · Crystal structure of human juno (crystal form 1) · the same entry in another collection · chain A against A, TM-score 1.00
  • A6ND01 · AlphaFold monomer V2.0 prediction for sperm-egg fusion protein juno (A6ND01) · a predicted model of the same protein · chain B against A, TM-score 0.97

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