› 3fe7

X-ray diffraction
1.35Å resolution

Crystal Structure of HdmX bound to the p53-peptidomimetic Ac-Phe-Met-Aib-Pmp-Trp-Glu-Ac3c-Leu-NH2 at 1.35A

Released:
DOI: 10.2210/pdb3fe7/pdb
PDB entry 3fe7 coloured by chain, front view.
PDB entry 3fe7 coloured by chain, side view.
PDB entry 3fe7 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal Structures of Human MdmX (HdmX) in Complex with p53 Peptide Analogues Reveal Surprising Conformational Changes.
Kallen J, Goepfert A, Blechschmidt A, Izaac A, Geiser M, Tavares G, Ramage P, Furet P, Masuya K, Lisztwan J
J Biol Chem 284 8812-21 (2009)
PMID: 19153082

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-127316 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Protein Mdm4 Chain: A
Molecule details ›
Chain: A
Length: 100 amino acids
Theoretical weight: 11.19 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O15151 (Residues: 14-111; Coverage: 20%)
Gene names: MDM4, MDMX
Structure domains: SWIB/MDM2 domain
p53-peptidomimetic Ac-Phe-Met-Aib-Pmp-Trp-Glu-Ac3c-Leu-NH2 Chain: L
Molecule details ›
Chain: L
Length: 10 amino acids
Theoretical weight: 1.16 KDa
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

No bound ligands
3 modified residues:
Ligand AIB 1 x AIB
Ligand PM3 1 x PM3
Ligand 1AC 1 x 1AC

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P41
Unit cell:
a: 43.294Å b: 43.294Å c: 65.59Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.192 0.209
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

6 review citations

The tumor suppressor p53: from structures to drug discovery.
Joerger et al. (2010)
5 more

7 mentions without citation

Interfacial Peptides as Affinity Modulating Agents of Protein-Protein Interactions.
Ershov et al. (2022)
6 more