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Crystal structure of the MLL5 phd finger in complex with H3K4ME3

Analyse Crystal structure of the MLL5 phd finger in complex with H3K4ME3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4L58
Type: protein
Length: 72 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Histone-lysine N-methyltransferase MLL5; Histone H3 peptide
EC: 2.1.1.43
UniProt: Q8IZD2
Ligands: ZN

Structure

x-ray diffraction · 2 distinct chains · 18% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Histone-lysine N-methyltransferase MLL5 (EC 2.1.1.43)	protein	65	20% helix, 11% strand	Q8IZD2
B	Histone H3 peptide	protein	7	0% helix, 29% strand	—

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A

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

Interfaces

1 interface between chains.

A–B · 454 Å² buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (methylation).

Compared structures

4L58 · Crystal structure of the MLL5 PHD finger in complex with H3K4me3 · the same entry in another collection · chain A against A, TM-score 1.00
Q8IZD2 · AlphaFold monomer V2.0 prediction for inactive histone-lysine N-methyltransferase 2E… · a predicted model of the same protein · chain A against A, TM-score 0.96

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 Q8IZD2
Elsewhere: RCSB PDB 4L58 · PDBe 4L58 · UniProt Q8IZD2

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