› 5ecg

X-ray diffraction
3Å resolution

Crystal structure of the BRCT domains of 53BP1 in complex with p53 and H2AX-pSer139 (gammaH2AX)

Released:
DOI: 10.2210/pdb5ecg/pdb
PDB entry 5ecg coloured by chain, front view.
PDB entry 5ecg coloured by chain, side view.
PDB entry 5ecg coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
ATM Localization and Heterochromatin Repair Depend on Direct Interaction of the 53BP1-BRCT2 Domain with γH2AX.
Baldock RA, Day M, Wilkinson OJ, Cloney R, Jeggo PA, Oliver AW, Watts FZ, Pearl LH
Cell Rep 13 2081-9 (2015)
PMID: 26628370

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-138113 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Cellular tumor antigen p53 Chains: A, B
Molecule details ›
Chains: A, B
Length: 225 amino acids
Theoretical weight: 25.18 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P04637 (Residues: 95-312; Coverage: 56%)
Gene names: P53, TP53
Sequence domains: P53 DNA-binding domain
Structure domains: Immunoglobulin-like
TP53-binding protein 1 Chains: C, D
Molecule details ›
Chains: C, D
Length: 262 amino acids
Theoretical weight: 29.62 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q12888 (Residues: 1713-1972; Coverage: 13%)
Gene name: TP53BP1
Sequence domains: BRCA1 C Terminus (BRCT) domain
Structure domains: BRCT domain
SEP-GLN-GLU-TYR Chains: E, F
Molecule details ›
Chains: E, F
Length: 4 amino acids
Theoretical weight: 605 Da
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

1 bound ligand:
Ligand ZN 2 x ZN
1 modified residue:
Ligand SEP 2 x SEP

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P212121
Unit cell:
a: 70.264Å b: 94.498Å c: 131.742Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.207 0.204 0.264
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

20 review citations

DNA damage response signaling pathways and targets for radiotherapy sensitization in cancer.
Huang et al. (2020)
19 more

2 mentions without citation

Phosphorylation-dependent assembly of DNA damage response systems and the central roles of TOPBP1.
Day et al. (2021)
1 more