Solution NMR

Structural basis for histone code recognition by BRPF2-PHD1 finger

Source organism: Homo sapiens
Entry authors: Qin S, Zhang J, Wu J, Shi Y

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Bromodomain-containing protein 1; Histone H3.3 Chain: A
Molecule details ›
Chain: A
Length: 88 amino acids
Theoretical weight: 9.79 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: O95696 (Residues: 205-269; Coverage: 6%)
  • Canonical: P84243 (Residues: 2-16; Coverage: 11%)
Gene names: BRD1, BRL, BRPF2, H3-3A, H3-3B, H3.3A, H3.3B, H3F3, H3F3A, H3F3B, PP781
Sequence domains: PHD-finger
Structure domains: Zinc/RING finger domain, C3HC4 (zinc finger)

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing, torsion angle dynamics
Chemical shifts: BMR17244  
Expression system: Escherichia coli