MolNFT v1 · #90746 · protein

X-ray structure of WDR5-MLL1 win motif peptide binary complex

4ESG · Wd repeat-containing protein 5: “X-ray structure of WDR5-MLL1 win motif peptide binary complex”. X-ray diffraction, 3 pockets (best druggability 0.74). MolNFT v1 #90746 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4ESG
Type: protein
Length: 640 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Wd repeat-containing protein 5; Histone-lysine N-methyltransferase mll
EC: 2.1.1.43
UniProt: P61964, Q03164
Pockets: 3 · best druggability 0.74

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Wd repeat-containing protein 5	protein	304	0% helix, 51% strand	P61964
C, D	Histone-lysine N-methyltransferase mll (EC 2.1.1.43)	protein	16	19% helix, 0% strand	Q03164

Pockets

3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	456	0.74	0.83	43	empty
2	446	0.73	0.82	44	empty
3	419	0.58	0.75	55	empty

Interfaces

3 interfaces between chains.

A–D · 699 Å² buried · 11 hydrogen bonds · protein-protein
B–C · 697 Å² buried · 11 hydrogen bonds · protein-protein
A–B · 292 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

4ESG · X-ray structure of WDR5-MLL1 Win motif peptide binary complex · 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 4ESG · PDBe 4ESG · UniProt P61964 · UniProt Q03164

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