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X-ray structure of WDR5-MLL3 win motif peptide binary complex

Analyse X-ray structure of WDR5-MLL3 win motif peptide binary complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4ERY
Type
protein
Length
318 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Wd repeat-containing protein 5; Histone-lysine N-methyltransferase MLL3
EC
2.1.1.43
UniProt
P61964, Q8NEZ4
Pockets
1 · best druggability 0.74

Structure

x-ray diffraction · 2 distinct chains · 0% helix, 49% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AWd repeat-containing protein 5protein3040% helix, 51% strandP61964
DHistone-lysine N-methyltransferase MLL3 (EC 2.1.1.43)protein140% helix, 0% strandQ8NEZ4

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14770.740.8343empty

Interfaces

1 interface between chains.

  • A–D · 667 Ų buried · 10 hydrogen bonds · protein-protein

Compared structures

  • 4ERY · X-ray structure of WDR5-MLL3 Win motif peptide binary complex · the same entry in another collection · chain A against A, TM-score 1.00

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