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Mouse ZNRF3 ectodomain crystal form III

Analyse Mouse ZNRF3 ectodomain crystal form III in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4C8C
Type
protein
Length
290 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
E3 ubiquitin-protein ligase ZNRF3
EC
6.3.2.-
UniProt
Q5SSZ7
Pockets
4 · best druggability 0.54

Structure

x-ray diffraction · 2 distinct chains · 22% helix, 38% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AE3 ubiquitin-protein ligase ZNRF3 (EC 6.3.2.-)protein14622% helix, 38% strandQ5SSZ7
BE3 ubiquitin-protein ligase ZNRF3 (EC 6.3.2.-)protein14422% helix, 38% strandQ5SSZ7

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11160.540.8224empty
2790.460.8216empty
3650.430.8115empty
41020.370.7517empty

Interfaces

1 interface between chains.

  • A–B · 1174 Ų buried · 26 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

  • 4C8C · mouse ZNRF3 ectodomain crystal form III · the same entry in another collection · chain A against A, TM-score 1.00
  • Q5SSZ7 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase ZNRF3 (Q5SSZ7) · a predicted model of the same protein · chain A against A, TM-score 0.97

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