› 7bre

X-ray diffraction
2.8Å resolution

The crystal structure of MLL2 in complex with ASH2L and RBBP5

Released:
DOI: 10.2210/pdb7bre/pdb
PDB entry 7bre coloured by chain, front view.
PDB entry 7bre coloured by chain, side view.
PDB entry 7bre coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal Structure of MLL2 Complex Guides the Identification of a Methylation Site on P53 Catalyzed by KMT2 Family Methyltransferases.
Li Y, Zhao L, Tian X, Peng C, Gong F, Chen Y
Structure 28 1141-1148.e4 (2020)
PMID: 32697937

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:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-172253 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Set1/Ash2 histone methyltransferase complex subunit ASH2 Chains: A, D
Molecule details ›
Chains: A, D
Length: 184 amino acids
Theoretical weight: 20.6 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9UBL3 (Residues: 380-496, 516-598; Coverage: 28%)
Gene names: ASH2L, ASH2L1
Sequence domains: SPRY domain
Histone-lysine N-methyltransferase 2B Chains: B, E
Molecule details ›
Chains: B, E
Length: 165 amino acids
Theoretical weight: 19.04 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9UMN6 (Residues: 2551-2715; Coverage: 6%)
Gene names: HRX2, KIAA0304, KMT2B, MLL2, MLL4, TRX2, WBP7
Sequence domains: SET domain
Retinoblastoma-binding protein 5 Chains: C, F
Molecule details ›
Chains: C, F
Length: 27 amino acids
Theoretical weight: 3.26 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q15291 (Residues: 330-356; Coverage: 5%)
Gene names: RBBP5, RBQ3

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL19U1
Spacegroup: P21
Unit cell:
a: 79.075Å b: 66.195Å c: 83.734Å
α: 90° β: 93.23° γ: 90°
R-values:
R R work R free
0.221 0.218 0.265
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

Emerging and converging molecular mechanisms in dystonia.
Gonzalez-Latapi et al. (2021)
5 more