MDM2 bound to the transactivation domain of P53. Determined by X-ray diffraction at 2.6 Å resolution. Released 19 Nov 1997.
Explore 1YCR in 3D Show helices and sheets RCSB PDB PDBe
1YCR 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 | 27-28 | 2 | 1 |
| β-strand | 29-30 | 2 | 2 |
| α-helix | 32-39 | 8 | |
| β-strand | 48-49 | 2 | 1 |
| α-helix | 50-63 | 14 | |
| β-strand | 67 | 1 | 3 |
| β-strand | 74-76 | 3 | 3 |
| α-helix | 81-86 | 6 | |
| β-strand | 90-92 | 3 | 3 |
| α-helix | 96-105 | 10 | |
| β-strand | 107-108 | 2 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 19-23 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| MDM2 | A | protein | 109 | Homo sapiens | Q00987 (AlphaFold model) |
| P53 | B | protein | 15 | P04637 (AlphaFold model) |
>1YCR_1 MDM2 (chains A) SQIPASEQETLVRPKPLLLKLLKSVGAQKDTYTMKEVLFYLGQYIMTKRLYDEKQQHIVY CSNDLLGDLFGVPSFSVKEHRKIYTMIYRNLVVVNQQESSDSGTSVSEN
>1YCR_2 P53 (chains B) SQETFSDLWKLLPEN
Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain. Kussie, P.H., Gorina, S., Marechal, V. et al. Science (1996) 274:948-953. DOI 10.1126/science.274.5289.948 · PubMed
Other PDB entries of the same protein (UniProt Q00987 (AlphaFold model), which also has an AlphaFold model), best resolution first:
1YCR is part of these collections:
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