› 3eqy

X-ray diffraction
1.63Å resolution

Crystal structure of human MDMX in complex with a 12-mer peptide inhibitor

Released:
DOI: 10.2210/pdb3eqy/pdb
PDB entry 3eqy coloured by chain, front view.
PDB entry 3eqy coloured by chain, side view.
PDB entry 3eqy coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for high-affinity peptide inhibition of p53 interactions with MDM2 and MDMX.
Pazgier M, Liu M, Zou G, Yuan W, Li C, Li C, Li J, Monbo J, Zella D, Tarasov SG, Lu W
Proc Natl Acad Sci U S A 106 4665-70 (2009)
PMID: 19255450

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-127315 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Protein Mdm4 Chains: A, B
Molecule details ›
Chains: A, B
Length: 85 amino acids
Theoretical weight: 9.58 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: O15151 (Residues: 24-108; Coverage: 17%)
Gene names: MDM4, MDMX
Structure domains: SWIB/MDM2 domain
12-mer peptide inhibitor Chains: C, D
Molecule details ›
Chains: C, D
Length: 12 amino acids
Theoretical weight: 1.43 KDa
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

2 bound ligands:
Ligand GAI 2 x GAI
Ligand PO4 4 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P31
Unit cell:
a: 75.627Å b: 75.627Å c: 35.181Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.156 0.155 0.169
Expression system: Not provided

Quick links

Citations

45 review citations

MDM2, MDMX and p53 in oncogenesis and cancer therapy.
Wade et al. (2013)
44 more

14 mentions without citation

p53-based cancer therapy.
Lane et al. (2010)
13 more