› 1muf

X-ray diffraction
2.26Å resolution

Structure of histone H3 K4-specific methyltransferase SET7/9

Released:
DOI: 10.2210/pdb1muf/pdb
PDB entry 1muf coloured by chain, front view.
PDB entry 1muf coloured by chain, side view.
PDB entry 1muf coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The active site of the SET domain is constructed on a knot.
Jacobs SA, Harp JM, Devarakonda S, Kim Y, Rastinejad F, Khorasanizadeh S
Nat Struct Biol 9 833-8 (2002)
PMID: 12389038

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:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-186700 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone-lysine N-methyltransferase SETD7 Chain: A
Molecule details ›
Chain: A
Length: 257 amino acids
Theoretical weight: 28.94 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8WTS6 (Residues: 81-337; Coverage: 70%)
Gene names: KIAA1717, KMT7, SET7, SET9, SETD7
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 6 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P6422
Unit cell:
a: 110.973Å b: 110.973Å c: 96.05Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.229 0.229 0.249
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

16 review citations

The SET-domain protein superfamily: protein lysine methyltransferases.
Dillon et al. (2005)
15 more

5 mentions without citation

Histone lysine methylation dynamics: establishment, regulation, and biological impact.
Black et al. (2012)
4 more