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Displacement of WDR5 from chromatin by a pharmacological win site inhibitor with picomolar affinity

Analyse Displacement of WDR5 from chromatin by a pharmacological win site inhibitor… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6E1Z
Type: protein
Length: 612 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Wd repeat-containing protein 5
UniProt: P61964
Ligands: HLP
Pockets: 2 · best druggability 0.80

Structure

x-ray diffraction · 2 distinct chains · 0% helix, 52% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Wd repeat-containing protein 5	protein	307	0% helix, 52% strand	P61964
B	Wd repeat-containing protein 5	protein	305	0% helix, 52% strand	P61964

Ligands and binding sites

HLP · 5-[(1H-imidazol-1-yl)methyl]furan-2-carboxylic acid · ligand · 2 copies · chains A, B

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

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	990	0.80	0.81	91	HLP
2	663	0.76	0.81	63	HLP

Interfaces

1 interface between chains.

A–B · 181 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

6E1Z · Displacement of WDR5 from chromatin by a pharmacological WIN site inhibitor with… · 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 6E1Z · PDBe 6E1Z · UniProt P61964

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