› 5f5e

X-ray diffraction
1.8Å resolution

The Crystal Structure of MLL1 SET domain with N3816I/Q3867L mutation

Released:
DOI: 10.2210/pdb5f5e/pdb
PDB entry 5f5e coloured by chain, front view.
PDB entry 5f5e coloured by chain, side view.
PDB entry 5f5e coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for activity regulation of MLL family methyltransferases.
Li Y, Han J, Zhang Y, Cao F, Liu Z, Li S, Wu J, Hu C, Wang Y, Shuai J, Chen J, Cao L, Li D, Shi P, Tian C, Zhang J, Dou Y, Li G, Chen Y, Lei M
Nature 530 447-52 (2016)
PMID: 26886794

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + a [histone H3]-L-lysine(4) = S-adenosyl-L-homocysteine + a [histone H3]-N(6)-methyl-L-lysine(4)
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169856 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
MLL cleavage product C180 Chain: A
Molecule details ›
Chain: A
Length: 158 amino acids
Theoretical weight: 18.24 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q03164 (Residues: 3813-3969; Coverage: 4%)
Gene names: ALL1, CXXC7, HRX, HTRX, KMT2A, MLL, MLL1, TRX1
Sequence domains: SET domain
Structure domains: SET domain

Ligands and Environments

2 bound ligands:
Ligand ZN 1 x ZN
Ligand SAH 1 x SAH
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL19U1
Spacegroup: P3221
Unit cell:
a: 54.574Å b: 54.574Å c: 104.656Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.204 0.202 0.236
Expression system: Escherichia coli

Quick links

Citations

35 review citations

Writing, erasing and reading histone lysine methylations.
Hyun et al. (2017)
34 more

3 mentions without citation

Activation and regulation of H2B-Ubiquitin-dependent histone methyltransferases.
Worden et al. (2019)
2 more