› 6ago

X-ray diffraction
3.1Å resolution

Crystal structure of MRG15-ASH1L Histone methyltransferase complex

Released:
DOI: 10.2210/pdb6ago/pdb
Model geometry
Fit model/data
PDB entry 6ago coloured by chain, front view.
PDB entry 6ago coloured by chain, side view.
PDB entry 6ago coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural Basis of MRG15-Mediated Activation of the ASH1L Histone Methyltransferase by Releasing an Autoinhibitory Loop.
Lee Y, Yoon E, Cho S, Schmähling S, Müller J, Song JJ
Structure 27 846-852.e3 (2019)
PMID: 30827841

Function and Biology Details

Reactions catalysed: 
(1a) S-adenosyl-L-methionine + a [histone H3]-L-lysine(36) = S-adenosyl-L-homocysteine + a [histone H3]-N(6)-methyl-L-lysine(36)
S-adenosyl-L-methionine + a [histone H3]-L-lysine(9) = S-adenosyl-L-homocysteine + a [histone H3]-N(6)-methyl-L-lysine(9)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192539 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Histone-lysine N-methyltransferase ASH1L Chains: A, B
Molecule details ›
Chains: A, B
Length: 256 amino acids
Theoretical weight: 30.01 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9NR48 (Residues: 2039-2293; Coverage: 9%)
Gene names: ASH1L, KIAA1420, KMT2H
Sequence domains:
Mortality factor 4-like protein 1 Chains: C, D
Molecule details ›
Chains: C, D
Length: 173 amino acids
Theoretical weight: 20.1 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UBU8 (Residues: 190-361; Coverage: 48%)
Gene names: FWP006, HSPC008, HSPC061, MORF4L1, MRG15, PP368
Sequence domains: MRG
Structure domains: MRG domain

Ligands and Environments

2 bound ligands:
Ligand SAM 1 x SAM
Ligand ZN 6 x ZN
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: PHOTON FACTORY BEAMLINE AR-NE3A
Spacegroup: P3112
Unit cell:
a: 115.757Å b: 115.757Å c: 209.282Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.224 0.22 0.272
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Structural and functional specificity of H3K36 methylation.
Lam et al. (2022)
2 more

2 mentions without citation

Allosteric regulation of histone lysine methyltransferases: from context-specific regulation to selective drugs.
Davidovich et al. (2021)
1 more

PDB-REDO

The sliders below show the change in model quality between original PDB entry and the PDB-REDO entry

Model Geometry
 
 
Data not available
DNA/RNA Geometry
 
 
Data not available
Fit model/data
 
 
Data not available
PDB-REDO