› 3mb3

X-ray diffraction
2.25Å resolution

Crystal Structure of the second bromodomain of Pleckstrin homology domain interacting protein (PHIP)

Released:
DOI: 10.2210/pdb3mb3/pdb
PDB 3mb3 coloured by chain and viewed from the front.
PDB 3mb3 coloured by chain and viewed from the side.
PDB 3mb3 coloured by chain and viewed from the top.
Source organism: Homo sapiens
Primary publication:
Histone recognition and large-scale structural analysis of the human bromodomain family.
Filippakopoulos P, Picaud S, Mangos M, Keates T, Lambert JP, Barsyte-Lovejoy D, Felletar I, Volkmer R, Müller S, Pawson T, Gingras AC, Arrowsmith CH, Knapp S
Cell 149 214-31 (2012)
PMID: 22464331

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:
PH-interacting protein Chain: A
Molecule details ›
Chain: A
Length: 135 amino acids
Theoretical weight: 16.13 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8WWQ0 (Residues: 1302-1434; Coverage: 7%)
Gene names: DCAF14, PHIP, WDR11
Sequence domains: Bromodomain
Structure domains: Bromodomain-like

Ligands and Environments

1 bound ligand:
Ligand MB3 1 x MB3
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P3121
Unit cell:
a: 92.09Å b: 92.09Å c: 76.12Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.208 0.206 0.257
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

210 review citations

A Comprehensive Review of BET Protein Biochemistry, Physiology, and Pathological Roles.
Ali et al. (2022)
209 more

9 mentions without citation

Druggability analysis and structural classification of bromodomain acetyl-lysine binding sites.
Vidler et al. (2012)
8 more