› 6u6k

X-ray diffraction
1.7Å resolution

BRD4-BD1 in complex with the cyclic peptide 3.1_3

Released:
DOI: 10.2210/pdb6u6k/pdb
PDB entry 6u6k coloured by chain, front view.
PDB entry 6u6k coloured by chain, side view.
PDB entry 6u6k 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
OpenAccess logo 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 dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130125 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Bromodomain-containing protein 4 Chain: A
Molecule details ›
Chain: A
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 3.1_3 Chain: C
Molecule details ›
Chain: C
Length: 13 amino acids
Theoretical weight: 1.47 KDa
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

No bound ligands
1 modified residue:
Ligand ALY 2 x ALY

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: C2
Unit cell:
a: 121.957Å b: 41.903Å c: 29.538Å
α: 90° β: 94.204° γ: 90°
R-values:
R R work R free
0.182 0.18 0.218
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

1 mention without citation

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