Crystal structure of human MDMX in complex with a 12-mer peptide inhibitor. Determined by X-ray diffraction at 1.63 Å resolution. Released 17 Mar 2009.
Explore 3EQY in 3D Show helices and sheets RCSB PDB PDBe
3EQY contains 10 α-helices and 14 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 | 66-67 | 2 | 3 |
| β-strand | 70-75 | 6 | 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 | 3-8 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Mdm4 protein | A, B | protein | 85 | Homo sapiens | O15151 (AlphaFold model) |
| 12-mer peptide inhibitor | C, D | protein | 12 |
>3EQY_1 Mdm4 protein (chains A, B) INQVRPKLPLLKILHAAGAQGEMFTVKEVMHYLGQYIMVKQLYDAAAQHMVYCGGDLLGE LLGRQSFSVKDPSPLYDMLRKNLVT
>3EQY_2 12-mer peptide inhibitor (chains C, D) TSFAEYWNLLSP
Structural basis for high-affinity peptide inhibition of p53 interactions with MDM2 and MDMX. Pazgier, M., Liu, M., Zou, G. et al. Proc Natl Acad Sci U S A (2009) 106:4665-4670. DOI 10.1073/pnas.0900947106 · 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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