› 6rkk

X-ray diffraction
1.88Å resolution

Fragment AZ-021 binding at the p53pT387/14-3-3 sigma interface

Released:
DOI: 10.2210/pdb6rkk/pdb
PDB entry 6rkk coloured by chain, front view.
PDB entry 6rkk coloured by chain, side view.
PDB entry 6rkk coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Fragment-based Differential Targeting of PPI Stabilizer Interfaces.
Guillory X, Wolter M, Leysen S, Neves JF, Kuusk A, Genet S, Somsen B, Morrow JK, Rivers E, van Beek L, Patel J, Goodnow R, Schoenherr H, Fuller N, Cao Q, Doveston RG, Brunsveld L, Arkin MR, Castaldi P, Boyd H, Landrieu I, Chen H, Ottmann C
OpenAccess logo J Med Chem 63 6694-6707 (2020)
PMID: 32501690

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138132 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
14-3-3 protein sigma Chain: A
Molecule details ›
Chain: A
Length: 253 amino acids
Theoretical weight: 28.21 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P31947 (Residues: 1-248; Coverage: 100%)
Gene names: HME1, SFN
Sequence domains: 14-3-3 protein
Cellular tumor antigen p53 Chain: P
Molecule details ›
Chain: P
Length: 12 amino acids
Theoretical weight: 1.45 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P04637 (Residues: 382-393; Coverage: 3%)
Gene names: P53, TP53

Ligands and Environments

4 bound ligands:
Ligand MG 2 x MG
Ligand CL 1 x CL
Ligand GOL 1 x GOL
Ligand K6W 1 x K6W
1 modified residue:
Ligand TPO 1 x TPO

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-003
Spacegroup: C2221
Unit cell:
a: 82.12Å b: 112.42Å c: 62.62Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.194 0.272
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

9 review citations

Fragment-to-Lead Medicinal Chemistry Publications in 2020.
de Esch et al. (2022)
8 more