Structure of human MDMX in complex with high affinity peptide. Determined by X-ray diffraction at 1.4 Å resolution. Released 16 Dec 2008.
Explore 3FDO in 3D Show helices and sheets RCSB PDB PDBe
3FDO contains 5 α-helices and 6 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 27-29 | 3 | 1 |
| α-helix | 31-38 | 8 | |
| β-strand | 47 | 1 | 1 |
| α-helix | 49-63 | 15 | |
| β-strand | 66-67 | 2 | 2 |
| β-strand | 70-75 | 6 | 2 |
| α-helix | 80-85 | 6 | |
| β-strand | 89-91 | 3 | 2 |
| α-helix | 96-105 | 10 | |
| β-strand | 106-108 | 3 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 19-24 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein Mdm4 | A | protein | 90 | Homo sapiens | O15151 (AlphaFold model) |
| Synthetic high affinity peptide | B | protein | 12 |
>3FDO_1 Protein Mdm4 (chains A) IQINQVRPKLPLLKILHAAGAQGEMFTVKEVMHYLGQYIMVKQLYDQQEQHMVYCGGDLL GELLGRQSFSVKDPSPLYDMLRKNLVTLAT
>3FDO_2 Synthetic high affinity peptide (chains B) LTFEHYWAQLTS
| ID | Name | Formula | Copies |
|---|---|---|---|
| MG | Magnesium ion | Mg | 5 |
High affinity interaction of the p53 peptide-analogue with human Mdm2 and Mdmx. Czarna, A., Popowicz, G.M., Pecak, A. et al. Cell Cycle (2009) 8:1176-1184. DOI 10.4161/cc.8.8.8185 · PubMed
Other PDB entries of the same protein (UniProt O15151 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 3FDO directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.