Human MDMX liganded with a 12mer peptide inhibitor (pDI6W). Determined by X-ray diffraction at 1.74 Å resolution. Released 10 Nov 2009.
Explore 3JZP in 3D Show helices and sheets RCSB PDB PDBe
3JZP contains 5 α-helices and 7 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 | 26-27 | 2 | 1 |
| β-strand | 28-29 | 2 | 2 |
| α-helix | 31-39 | 9 | |
| β-strand | 47-48 | 2 | 1 |
| α-helix | 49-62 | 14 | |
| β-strand | 66 | 1 | 3 |
| β-strand | 73-75 | 3 | 3 |
| α-helix | 80-85 | 6 | |
| β-strand | 89-91 | 3 | 3 |
| α-helix | 96-105 | 10 | |
| β-strand | 106-107 | 2 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 19-24 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein Mdm4 | A | protein | 89 | Homo sapiens | O15151 (AlphaFold model) |
| pDI6W peptide (12mer) | P | protein | 12 |
>3JZP_1 Protein Mdm4 (chains A) QINQVRPKLPLLKILHAAGAQGEMFTVKEVMHYLGQYIMVKQLYDQQEQHMVYCGGDLLG ELLGRQSFSVKDPSPLYDMLRKNLVTLAT
>3JZP_2 pDI6W peptide (12mer) (chains P) LTFEHWWAQLTS
Structure-based design of high affinity peptides inhibiting the interaction of p53 with MDM2 and MDMX. Phan, J., Li, Z., Kasprzak, A. et al. J Biol Chem (2010) 285:2174-2183. DOI 10.1074/jbc.M109.073056 · PubMed
Other PDB entries of the same protein (UniProt O15151 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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