Research workbench

WDR5 in complex with myc site fragment inhibitor

Analyse WDR5 in complex with myc site fragment inhibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6UHY
Type: protein
Length: 605 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: WDR5
UniProt: P61964
Ligands: Q8G
Pockets: 6 · best druggability 0.82

Structure

x-ray diffraction · 2 distinct chains · 0% helix, 51% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	WDR5	protein	301	0% helix, 53% strand	P61964
B	WDR5	protein	304	0% helix, 50% strand	P61964

Ligands and binding sites

Q8G · 1-cyclohexyl-1H-benzimidazole-5-carboxylic acid · ligand · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	930	0.82	0.83	76	empty
2	491	0.74	0.82	46	empty
3	194	0.56	0.80	28	empty
4	175	0.51	0.78	19	empty
5	121	0.40	0.75	20	empty

Interfaces

1 interface between chains.

A–B · 445 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

6UHY · WDR5 in complex with Myc site fragment inhibitor · 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
Elsewhere: RCSB PDB 6UHY · PDBe 6UHY · UniProt P61964

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.