MolNFT v1 · #62461 · protein

Structure of WDR5 bound to MLL1 peptide

3EG6 · Wd repeat-containing protein 5: “Structure of WDR5 bound to MLL1 peptide”. X-ray diffraction, 2 ligands (ACE, SO4), 1 pocket (best druggability 0.74). MolNFT v1 #62461 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3EG6
Type: protein
Length: 313 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Wd repeat-containing protein 5; Mll-1 peptide
UniProt: P61964, Q03164
Ligands: ACE, SO4
Pockets: 1 · best druggability 0.74

Structure

x-ray diffraction · 2 distinct chains · 1% helix, 50% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Wd repeat-containing protein 5	protein	304	0% helix, 52% strand	P61964
C	Mll-1 peptide	protein	9	33% helix, 0% strand	Q03164

Ligands and binding sites

ACE · Acetyl group · ligand · chains A, C
SO4 · Sulfate ion · ion · 3 copies · chains A

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

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	501	0.74	0.82	46	empty

Interfaces

1 interface between chains.

A–C · 603 Å² buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

3EG6 · Structure of WDR5 bound to MLL1 peptide · 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 Q03164
Elsewhere: RCSB PDB 3EG6 · PDBe 3EG6 · UniProt P61964 · UniProt Q03164

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