› 3cbp

X-ray diffraction
1.42Å resolution

Set7/9-ER-Sinefungin complex

Released:
DOI: 10.2210/pdb3cbp/pdb
PDB entry 3cbp coloured by chain, front view.
PDB entry 3cbp coloured by chain, side view.
PDB entry 3cbp coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Regulation of estrogen receptor alpha by the SET7 lysine methyltransferase.
Subramanian K, Jia D, Kapoor-Vazirani P, Powell DR, Collins RE, Sharma D, Peng J, Cheng X, Vertino PM
Mol Cell 30 336-47 (2008)
PMID: 18471979

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:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136917 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Histone-lysine N-methyltransferase SETD7 Chain: A
Molecule details ›
Chain: A
Length: 256 amino acids
Theoretical weight: 28.56 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8WTS6 (Residues: 111-366; Coverage: 70%)
Gene names: KIAA1717, KMT7, SET7, SET9, SETD7
Sequence domains:
Structure domains:
Estrogen receptor Chain: B
Molecule details ›
Chain: B
Length: 10 amino acids
Theoretical weight: 1.15 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P03372 (Residues: 298-307; Coverage: 2%)
Gene names: ESR, ESR1, NR3A1

Ligands and Environments

3 bound ligands:
Ligand SFG 1 x SFG
Ligand BME 3 x BME
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: P21212
Unit cell:
a: 102.042Å b: 38.786Å c: 66.571Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.239 0.239 0.243
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

72 review citations

Histone Modifications and Cancer.
Audia et al. (2016)
71 more

7 mentions without citation

Modulation of epigenetic targets for anticancer therapy: clinicopathological relevance, structural data and drug discovery perspectives.
Andreoli et al. (2013)
6 more