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Crystal structure of HERC2 zz domain in complex with histone H3 tail

Analyse Crystal structure of HERC2 zz domain in complex with histone H3 tail in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6WW4
Type: protein
Length: 112 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Histone H3.1,E3 ubiquitin-protein ligase HERC2
EC: 2.3.2.26
UniProt: P68431, O95714
Ligands: ZN

Structure

x-ray diffraction · 1 distinct chain · 11% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B, A	Histone H3.1,E3 ubiquitin-protein ligase HERC2 (EC 2.3.2.26)	protein	56	11% helix, 25% strand	P68431, O95714

Ligands and binding sites

ZN · Zinc ion · metal · 4 copies · chains B, A
GOL · Glycerol · additive · 2 copies · chains B, A

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

Interfaces

1 interface between chains.

B–A · 33 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

6WW4 · Crystal structure of HERC2 ZZ domain in complex with histone H3 tail · the same entry in another collection · chain B against B, TM-score 1.00
P68431 · AlphaFold monomer V2.0 prediction for histone H3.1 (P68431) · a predicted model of the same protein · chain A against A, TM-score 0.25

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 P68431
Every structure of UniProt O95714
Elsewhere: RCSB PDB 6WW4 · PDBe 6WW4 · UniProt P68431 · UniProt O95714

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