Crystal Structure of MDMX phosporylated Tyr99 in complex with a 12-mer peptide. Determined by X-ray diffraction at 1.55 Å resolution. Released 22 Jul 2015.
Explore 4RXZ in 3D Show helices and sheets RCSB PDB PDBe
4RXZ contains 10 α-helices and 15 β-strands across 4 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 | 1 | 1 |
| β-strand | 28-29 | 2 | 2 |
| α-helix | 31-39 | 9 | |
| β-strand | 47 | 1 | 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 |
|---|---|---|---|
| β-strand | 27 | 1 | 4 |
| β-strand | 28-29 | 2 | 5 |
| α-helix | 31-39 | 9 | |
| β-strand | 47 | 1 | 4 |
| α-helix | 49-62 | 14 | |
| β-strand | 66 | 1 | 6 |
| β-strand | 73-75 | 3 | 6 |
| α-helix | 80-85 | 6 | |
| β-strand | 89-91 | 3 | 6 |
| β-strand | 94 | 1 | 6 |
| α-helix | 96-105 | 10 | |
| β-strand | 106-107 | 2 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-7 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein Mdm4 | A, B | protein | 85 | Homo sapiens | O15151 (AlphaFold model) |
| 12-mer peptide inhibitor | C, D | protein | 12 |
>4RXZ_1 Protein Mdm4 (chains A, B) INQVRPKLPLLKILHAAGAQGEMFTVKEVMHYLGQYIMVKQLYDQQEQHMVYCGGDLLGE LLGRQSFSVKDPSPLYDMLRKNLVT
>4RXZ_2 12-MER PEPTIDE INHIBITOR (chains C, D) TSFAEYWNLLSP
Structural basis of how stress-induced MDMX phosphorylation activates p53. Chen, X., Gohain, N., Zhan, C. et al. Oncogene (2016) 35:1919-1925. DOI 10.1038/onc.2015.255 · 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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