› 6ulq

X-ray diffraction
2.7Å resolution

BRD2-BD1 in complex with the cyclic peptide 4.2_3

Released:
DOI: 10.2210/pdb6ulq/pdb
PDB entry 6ulq coloured by chain, front view.
PDB entry 6ulq coloured by chain, side view.
PDB entry 6ulq 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-150466 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Bromodomain-containing protein 2 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 136 amino acids
Theoretical weight: 15.89 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P25440 (Residues: 65-194; Coverage: 16%)
Gene names: BRD2, KIAA9001, RING3
Sequence domains: Bromodomain
Cyclic peptide 4.2_3 Chains: D, E, F
Molecule details ›
Chains: D, E, F
Length: 18 amino acids
Theoretical weight: 2.21 KDa
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Unit cell:
a: 80.484Å b: 76.142Å c: 109.661Å
α: 90° β: 108.275° γ: 90°
R-values:
R R work R free
0.223 0.222 0.252
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

3 review citations

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

1 mention without citation

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