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Crystal structure of WDR5 in complex with the WDR5-interacting motif of MLL4

Analyse Crystal structure of WDR5 in complex with the WDR5-interacting motif of MLL4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3UVM
Type: protein
Length: 314 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 MLL4
EC: 2.1.1.43
UniProt: P61964, Q9UMN6
Pockets: 1 · best druggability 0.73

Structure

x-ray diffraction · 2 distinct chains · 1% helix, 49% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Wd repeat-containing protein 5	protein	304	0% helix, 51% strand	P61964
B	Histone-lysine N-methyltransferase MLL4 (EC 2.1.1.43)	protein	10	30% helix, 0% strand	Q9UMN6

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	490	0.73	0.82	46	empty

Interfaces

1 interface between chains.

A–B · 746 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

3UVM · Crystal structure of WDR5 in complex with the WDR5-interacting motif of MLL4 · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P61964
Every structure of UniProt Q9UMN6
Elsewhere: RCSB PDB 3UVM · PDBe 3UVM · UniProt P61964 · UniProt Q9UMN6

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