1YCR: MDM2

MDM2 bound to the transactivation domain of P53. Determined by X-ray diffraction at 2.6 Å resolution. Released 19 Nov 1997.

Method
X-ray diffraction
Resolution
2.6 Å
Organism
Homo sapiens
Chains
2
Atoms
818
Mol. weight
14.34 kDa
Released
19 Nov 1997

Explore 1YCR in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 4 helices, 7 β-strands

ElementResiduesLengthSheet
β-strand27-2821
β-strand29-3022
α-helix32-398
β-strand48-4921
α-helix50-6314
β-strand6713
β-strand74-7633
α-helix81-866
β-strand90-9233
α-helix96-10510
β-strand107-10822
Chain B: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix19-235

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
MDM2Aprotein109Homo sapiensQ00987 (AlphaFold model)
P53Bprotein15P04637 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1YCR_1 MDM2 (chains A)
SQIPASEQETLVRPKPLLLKLLKSVGAQKDTYTMKEVLFYLGQYIMTKRLYDEKQQHIVY
CSNDLLGDLFGVPSFSVKEHRKIYTMIYRNLVVVNQQESSDSGTSVSEN
Sequence of entity 2 (B), FASTA
>1YCR_2 P53 (chains B)
SQETFSDLWKLLPEN

Primary citation

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:

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