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Crystal structure of the KH2 domain of human RNA-binding E3 ubiquitin- protein ligase mex-3C

Analyse Crystal structure of the KH2 domain of human RNA-binding E3 ubiquitin- protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5WWZ
Type
protein
Length
237 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
RNA-binding E3 ubiquitin-protein ligase MEX3C
EC
2.3.2.27
UniProt
Q5U5Q3
Ligands
SO4
Pockets
3 · best druggability 0.62

Structure

x-ray diffraction · 3 distinct chains · 43% helix, 23% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
BRNA-binding E3 ubiquitin-protein ligase MEX3C (EC 2.3.2.27)protein8043% helix, 19% strandQ5U5Q3
ARNA-binding E3 ubiquitin-protein ligase MEX3C (EC 2.3.2.27)protein7845% helix, 26% strandQ5U5Q3
CRNA-binding E3 ubiquitin-protein ligase MEX3C (EC 2.3.2.27)protein7943% helix, 25% strandQ5U5Q3

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 4 copies · chains B, A, C

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13070.620.7934SO4
2730.300.7318empty
3590.300.7517empty

Interfaces

3 interfaces between chains.

  • A–C · 872 Ų buried · 24 hydrogen bonds · protein-protein
  • B–A · 558 Ų buried · 5 hydrogen bonds · protein-protein
  • B–C · 105 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 5WWZ · Crystal structure of the KH2 domain of human RNA-binding E3 ubiquitin-protein ligase… · the same entry in another collection · chain B against B, TM-score 1.00
  • Q5U5Q3 · AlphaFold monomer V2.0 prediction for RNA-binding E3 ubiquitin- protein ligase MEX3C… · a predicted model of the same protein · chain A against A, TM-score 0.89

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