› 6ulv

X-ray diffraction
2.2Å resolution

BRD4-BD1 in complex with the cyclic peptide 4.2_1

Released:
DOI: 10.2210/pdb6ulv/pdb
PDB entry 6ulv coloured by chain, front view.
PDB entry 6ulv coloured by chain, side view.
PDB entry 6ulv coloured by chain, top view.
Source organisms:
Primary publication:
Cyclic peptides can engage a single binding pocket through highly divergent modes.
Patel K, Walport LJ, Walshe JL, Solomon PD, Low JKK, Tran DH, Mouradian KS, Silva APG, Wilkinson-White L, Norman A, Franck C, Matthews JM, Guss JM, Payne RJ, Passioura T, Suga H, Mackay JP
Proc Natl Acad Sci U S A 117 26728-26738 (2020)
PMID: 33046654

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130151 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Bromodomain-containing protein 4 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 146 amino acids
Theoretical weight: 17.2 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O60885 (Residues: 42-168; Coverage: 9%)
Gene names: BRD4, HUNK1
Sequence domains: Bromodomain
Cyclic peptide 4.2_3 Chains: E, G
Molecule details ›
Chains: E, G
Length: 16 amino acids
Theoretical weight: 2.1 KDa
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

3 bound ligands:
Ligand IOD 7 x IOD
Ligand B3P 1 x B3P
Ligand GOL 2 x GOL
1 modified residue:
Ligand ALY 6 x ALY

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: P6522
Unit cell:
a: 112.288Å b: 112.288Å c: 235.579Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.2 0.198 0.238
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

2 review citations

Cyclisation strategies for stabilising peptides with irregular conformations.
Vu et al. (2021)
1 more

2 mentions without citation

Cyclic peptides can engage a single binding pocket through highly divergent modes.
Patel et al. (2020)
1 more