PDBsum entry 3muk

Signaling protein

PDB id: 3muk

Contents

Protein chain

127 a.a. *

Ligands

ALA-THR-PRK-ALA-ALA-ARG-LYS

EDO

Waters ×151

* Residue conservation analysis

PDB id:

3muk

Name:

Signaling protein

Title:

Crystal structure of brd4 bromodomain 1 with propionylated histone h3- k(prop)23

Structure:

Bromodomain-containing protein 4. Chain: a. Fragment: bromodomain, unp residues 42-168. Synonym: mitotic chromosome-associated protein, mcap. Engineered: yes. Peptide of histone h3.3. Chain: d. Fragment: histone h3 peptide, unp residues 22-29. Engineered: yes

Source:

Mus musculus. Mouse. Organism_taxid: 10090. Gene: brd4, mcap. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Other_details: fmoc solid phase synthesis

Resolution:

1.75Å R-factor: 0.175 R-free: 0.219

Authors:

F.Vollmuth,M.Geyer

Key ref:

F.Vollmuth and M.Geyer (2010). Interaction of propionylated and butyrylated histone H3 lysine marks with Brd4 bromodomains. Angew Chem Int Ed Engl, 49, 6768-6772. PubMed id: 20715035

Date:

03-May-10 Release date: 11-Aug-10

Protein chain

Q9ESU6  (BRD4_MOUSE) -  Bromodomain-containing protein 4 from Mus musculus

Seq: 1400 a.a.

Struc: 127 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.?

Angew Chem Int Ed Engl 49:6768-6772 (2010)

PubMed id: 20715035

Interaction of propionylated and butyrylated histone H3 lysine marks with Brd4 bromodomains.

F.Vollmuth, M.Geyer.

ABSTRACT

No abstract given.