4RXZ: MDMX phosporylated Tyr99

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.

Method
X-ray diffraction
Resolution
1.55 Å
Organism
Homo sapiens
Chains
4
Atoms
1,655
Mol. weight
22.51 kDa
Released
22 Jul 2015

Explore 4RXZ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 4 helices, 7 β-strands

ElementResiduesLengthSheet
β-strand2711
β-strand28-2922
α-helix31-399
β-strand4711
α-helix49-6214
β-strand6613
β-strand73-7533
α-helix80-856
β-strand89-9133
α-helix96-10510
β-strand106-10722
Chain B: 4 helices, 8 β-strands
ElementResiduesLengthSheet
β-strand2714
β-strand28-2925
α-helix31-399
β-strand4714
α-helix49-6214
β-strand6616
β-strand73-7536
α-helix80-856
β-strand89-9136
β-strand9416
α-helix96-10510
β-strand106-10725
Chains C and D: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix3-75

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Protein Mdm4A, Bprotein85Homo sapiensO15151 (AlphaFold model)
12-mer peptide inhibitorC, Dprotein12
Sequence of entity 1 (A, B), FASTA
>4RXZ_1 Protein Mdm4 (chains A, B)
INQVRPKLPLLKILHAAGAQGEMFTVKEVMHYLGQYIMVKQLYDQQEQHMVYCGGDLLGE
LLGRQSFSVKDPSPLYDMLRKNLVT
Sequence of entity 2 (C, D), FASTA
>4RXZ_2 12-MER PEPTIDE INHIBITOR (chains C, D)
TSFAEYWNLLSP

Primary citation

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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