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Structural basis of WDR5-mll interaction

Analyse Structural basis of WDR5-mll interaction in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3EMH
Type: protein
Length: 306 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Wd repeat-containing protein 5; Mixed-lineage leukemia protein 1
UniProt: P61964, Q59FF2
Ligands: SO4
Pockets: 2 · best druggability 0.74

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Wd repeat-containing protein 5	protein	300	0% helix, 52% strand	P61964
B	Mixed-lineage leukemia protein 1	protein	6	0% helix, 0% strand	Q59FF2

Ligands and binding sites

SO4 · Sulfate ion · ion · 2 copies · chains A

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	500	0.74	0.83	45	SO4
2	51	0.65	0.95	18	empty

Interfaces

1 interface between chains.

A–B · 514 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

3EMH · Structural basis of WDR5-MLL interaction · 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 Q59FF2
Elsewhere: RCSB PDB 3EMH · PDBe 3EMH · UniProt P61964 · UniProt Q59FF2

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