3FDO: Human MDMX

Structure of human MDMX in complex with high affinity peptide. Determined by X-ray diffraction at 1.4 Å resolution. Released 16 Dec 2008.

Method
X-ray diffraction
Resolution
1.4 Å
Organism
Homo sapiens
Chains
2
Atoms
988
Mol. weight
11.89 kDa
Ligands
MG
Released
16 Dec 2008

Explore 3FDO in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3FDO contains 5 α-helices and 6 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, 6 β-strands

ElementResiduesLengthSheet
β-strand27-2931
α-helix31-388
β-strand4711
α-helix49-6315
β-strand66-6722
β-strand70-7562
α-helix80-856
β-strand89-9132
α-helix96-10510
β-strand106-10831
Chain B: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix19-246

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Protein Mdm4Aprotein90Homo sapiensO15151 (AlphaFold model)
Synthetic high affinity peptideBprotein12
Sequence of entity 1 (A), FASTA
>3FDO_1 Protein Mdm4 (chains A)
IQINQVRPKLPLLKILHAAGAQGEMFTVKEVMHYLGQYIMVKQLYDQQEQHMVYCGGDLL
GELLGRQSFSVKDPSPLYDMLRKNLVTLAT
Sequence of entity 2 (B), FASTA
>3FDO_2 Synthetic high affinity peptide (chains B)
LTFEHYWAQLTS

Ligands and cofactors

IDNameFormulaCopies
MGMagnesium ionMg5

Primary citation

High affinity interaction of the p53 peptide-analogue with human Mdm2 and Mdmx. Czarna, A., Popowicz, G.M., Pecak, A. et al. Cell Cycle (2009) 8:1176-1184. DOI 10.4161/cc.8.8.8185 · 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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