› 5jle

X-ray diffraction
2.4Å resolution

Crystal structure of SETD2 bound to SAH

Released:
DOI: 10.2210/pdb5jle/pdb
PDB entry 5jle coloured by chain, front view.
PDB entry 5jle coloured by chain, side view.
PDB entry 5jle coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Molecular basis for oncohistone H3 recognition by SETD2 methyltransferase.
Yang S, Zheng X, Lu C, Li GM, Allis CD, Li H
Genes Dev 30 1611-6 (2016)
PMID: 27474439

Function and Biology Details

Reaction 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)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189845 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone-lysine N-methyltransferase SETD2 Chain: A
Molecule details ›
Chain: A
Length: 279 amino acids
Theoretical weight: 32.04 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9BYW2 (Residues: 1434-1711; Coverage: 11%)
Gene names: HIF1, HSPC069, HYPB, KIAA1732, KMT3A, SET2, SETD2
Sequence domains:

Ligands and Environments

2 bound ligands:
Ligand ZN 3 x ZN
Ligand SAH 1 x SAH
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P212121
Unit cell:
a: 51.54Å b: 77.152Å c: 78.693Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.212 0.208 0.25
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

35 review citations

PRC2 is high maintenance.
Yu et al. (2019)
34 more

2 mentions without citation

Molecular basis for oncohistone H3 recognition by SETD2 methyltransferase.
Yang et al. (2016)
1 more