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Crystal structure of WDR5/HISTONE H3 complex

Analyse Crystal structure of WDR5/HISTONE H3 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2H13
Type: protein
Length: 308 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Wd-repeat protein 5; Histone H3 lys-4 dimethylated
UniProt: P61964
Pockets: 1 · best druggability 0.75

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Wd-repeat protein 5	protein	303	0% helix, 52% strand	P61964
B	Histone H3 lys-4 dimethylated	protein	5	0% helix, 0% strand	—

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	479	0.75	0.83	44	empty

Interfaces

1 interface between chains.

A–B · 467 Å² buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (methylation).

Compared structures

2H13 · Crystal structure of WDR5/histone H3 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
Elsewhere: RCSB PDB 2H13 · PDBe 2H13 · UniProt P61964

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