7cmz

X-ray diffraction
1.7Å resolution

Crystal Structure of BRCT7/8 in Complex with the APS Motif of PHF8

Released:

Function and Biology Details

Reactions catalysed:
(1a) a [histone H3]-N(6),N(6)-dimethyl-L-lysine(36) + 2-oxoglutarate + O(2) = a [histone H3]-N(6)-methyl-L-lysine(36) + succinate + formaldehyde + CO(2)
(1a) a [histone H3]-N(6),N(6)-dimethyl-L-lysine(9) + 2-oxoglutarate + O(2) = a [histone H3]-N(6)-methyl-L-lysine(9) + succinate + formaldehyde + CO(2)
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-187684 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
DNA topoisomerase 2-binding protein 1 Chain: A
Molecule details ›
Chain: A
Length: 230 amino acids
Theoretical weight: 26.06 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q92547 (Residues: 1264-1493; Coverage: 15%)
Gene names: KIAA0259, TOPBP1
Sequence domains: BRCA1 C Terminus (BRCT) domain
Histone lysine demethylase PHF8 Chain: B
Molecule details ›
Chain: B
Length: 22 amino acids
Theoretical weight: 2.42 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q9UPP1 (Residues: 842-863; Coverage: 2%)
Gene names: KIAA1111, PHF8, ZNF422

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL19U1
Spacegroup: P212121
Unit cell:
a: 54.517Å b: 60.35Å c: 66.03Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.178 0.215
Expression systems:
  • Escherichia coli
  • Not provided