8P0D: Human 14-3-3 sigma

Human 14-3-3 sigma in complex with human MDM2 peptide. Determined by X-ray diffraction at 1.31 Å resolution. Released 21 Feb 2024.

Method
X-ray diffraction
Resolution
1.31 Å
Organism
Homo sapiens
Chains
2
Atoms
2,459
Mol. weight
33.67 kDa
Ligands
MG
Released
21 Feb 2024

Explore 8P0D in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8P0D contains 15 α-helices and 2 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: 15 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix3-1513
α-helix19-3113
α-helix34-374
α-helix38-6932
α-helix80-10223
α-helix103-1075
α-helix108-1103
α-helix114-13421
α-helix135-1373
α-helix140-16122
α-helix167-17812
α-helix179-1835
α-helix187-20216
α-helix205-2073
α-helix210-23021
Chain B: 0 helices, 2 β-strands
ElementResiduesLengthSheet
β-strand165-16621
β-strand185-18621

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
14-3-3 protein sigmaAprotein259Homo sapiensP31947 (AlphaFold model)
E3 ubiquitin-protein ligase Mdm2Bprotein31Homo sapiensQ00987 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>8P0D_1 14-3-3 protein sigma (chains A)
MSYYHHHHHHDYDIPTTENLYFQGAMGSMERASLIQKAKLAEQAERYEDMAAFMKGAVEK
GEELSCEERNLLSVAYKNVVGGQRAAWRVLSSIEQKSNEEGSEEKGPEVREYREKVETEL
QGVCDTVLGLLDSHLIKEAGDAESRVFYLKMKGDYYRYLAEVATGDDKKRIIDSARSAYQ
EAMDISKKEMPPTNPIRLGLALNFSVFHYEIANSPEEAISLAKTTFDEAMADLHTLSEDS
YKDSTLIMQLLRDNLTLWT
Sequence of entity 2 (B), FASTA
>8P0D_2 E3 ubiquitin-protein ligase Mdm2 (chains B)
RRRAISETEENSDELSGERQRKRHKSDSISL

Ligands and cofactors

IDNameFormulaCopies
MGMagnesium ionMg2

Water and common crystallization additives (CL, PEG, GOL) are not listed.

Primary citation

Characterizing the protein-protein interaction between MDM2 and 14-3-3 sigma ; proof of concept for small molecule stabilization. Ward, J.A., Romartinez-Alonso, B., Kay, D.F. et al. J Biol Chem (2024) 300:105651-105651. DOI 10.1016/j.jbc.2024.105651 · PubMed

Other PDB entries of the same protein (UniProt P31947 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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