6Y1J: 14-3-3 sigma

14-3-3 sigma in complex with IkappaBalpha pS63 peptide. Determined by X-ray diffraction at 1.13 Å resolution. Released 4 Mar 2020.

Method
X-ray diffraction
Resolution
1.13 Å
Organism
Homo sapiens
Chains
2
Atoms
2,474
Mol. weight
30.69 kDa
Ligands
CA, MG
Released
4 Mar 2020

Explore 6Y1J in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6Y1J contains 14 α-helices and 0 β-strands across 1 chain. 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: 14 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix-3-04
α-helix3-1513
α-helix19-3113
α-helix34-374
α-helix38-6932
α-helix74-763
α-helix80-10223
α-helix103-1075
α-helix114-13421
α-helix140-16122
α-helix167-18216
α-helix187-20216
α-helix205-2073
α-helix210-23021

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
14-3-3 protein sigmaAprotein253Homo sapiensP31947 (AlphaFold model)
NF-kappa-B inhibitor alphaPprotein14Homo sapiensP25963 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>6Y1J_1 14-3-3 protein sigma (chains A)
GAMGSMERASLIQKAKLAEQAERYEDMAAFMKGAVEKGEELSCEERNLLSVAYKNVVGGQ
RAAWRVLSSIEQKSNEEGSEEKGPEVREYREKVETELQGVCDTVLGLLDSHLIKEAGDAE
SRVFYLKMKGDYYRYLAEVATGDDKKRIIDSARSAYQEAMDISKKEMPPTNPIRLGLALN
FSVFHYEIANSPEEAISLAKTTFDEAMADLHTLSEDSYKDSTLIMQLLRDNLTLWTADNA
GEEGGEAPQEPQS
Sequence of entity 2 (P), FASTA
>6Y1J_2 NF-kappa-B inhibitor alpha (chains P)
XQEVPRGSEPWKQQ

Ligands and cofactors

IDNameFormulaCopies
CACalcium ionCa2
MGMagnesium ionMg1

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

Primary citation

Interaction of an I kappa B alpha Peptide with 14-3-3. Wolter, M., Santo, D.L., Herman, P. et al. ACS Omega (2020) 5:5380-5388. DOI 10.1021/acsomega.9b04413 · PubMed

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

Browse structure collections

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