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Crystal structure of ENL (MLLT1) in complex with acetyllysine

Analyse Crystal structure of ENL (MLLT1) in complex with acetyllysine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6HPZ
Type: protein
Length: 140 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.3
Source: Homo sapiens
Molecule: Protein ENL
UniProt: Q03111
Ligands: ALY

Structure

x-ray diffraction · resolution 2.3 · 1 distinct chain · 9% helix, 51% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein ENL	protein	140	9% helix, 51% strand	Q03111

Ligands and binding sites

ALY · N(6)-acetyllysine · ligand · chains A
EDO · 1,2-ethanediol · additive · 2 copies · chains A

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

Compared structures

6HPZ · Crystal structure of enl (MLLT1) in complex with acetyllysine · the same entry in another collection · chain A against A, TM-score 1.00
Q03111 · AlphaFold monomer V2.0 prediction for protein enl (Q03111) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q03111
Elsewhere: RCSB PDB 6HPZ · PDBe 6HPZ · UniProt Q03111

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