› 5pr9

X-ray diffraction
1.82Å resolution

PanDDA analysis group deposition -- Crystal Structure of BRD1 after initial refinement with no ligand modelled (structure 82)

Released:
DOI: 10.2210/pdb5pr9/pdb
PDB 5pr9 coloured by chain and viewed from the front.
PDB 5pr9 coloured by chain and viewed from the side.
PDB 5pr9 coloured by chain and viewed from the top.
Source organism: Homo sapiens
Primary publication:
A multi-crystal method for extracting obscured crystallographic states from conventionally uninterpretable electron density.
Pearce NM, Krojer T, Bradley AR, Collins P, Nowak RP, Talon R, Marsden BD, Kelm S, Shi J, Deane CM, von Delft F
Nat Commun 8 15123 (2017)
PMID: 28436492

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bromodomain-containing protein 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 156 amino acids
Theoretical weight: 18.22 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O95696 (Residues: 555-688; Coverage: 13%)
Gene names: BRD1, BRL, BRPF2
Sequence domains: Bromodomain
Structure domains: Bromodomain-like

Ligands and Environments

2 bound ligands:
Ligand EDO 4 x EDO
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: P212121
Unit cell:
a: 55.38Å b: 56.458Å c: 102.147Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.179 0.216
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Advances in methods for atomic resolution macromolecular structure determination.
Thompson et al. (2020)
9 more