6Y3O: 14-3-3 Sigma

14-3-3 Sigma in complex with phosphorylated CAMKK2 peptide. Determined by X-ray diffraction at 1.5 Å resolution. Released 14 Oct 2020.

Method
X-ray diffraction
Resolution
1.5 Å
Organism
Homo sapiens
Chains
2
Atoms
2,275
Mol. weight
29.43 kDa
Ligands
MG, CA
Released
14 Oct 2020

Explore 6Y3O in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6Y3O contains 15 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: 15 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix3-1513
α-helix19-3113
α-helix34-374
α-helix38-6932
α-helix74-763
α-helix80-9819
α-helix103-1075
α-helix108-1103
α-helix114-13421
α-helix140-16122
α-helix167-17812
α-helix179-1835
α-helix187-20418
α-helix205-2073
α-helix210-23021

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
14-3-3 protein sigmaAprotein253Homo sapiensP31947 (AlphaFold model)
CAMKK2Pprotein8Homo sapiensQ96RR4 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>6Y3O_1 14-3-3 protein sigma (chains A)
GAMGSMERASLIQKAKLAEQAERYEDMAAFMKGAVEKGEELSCEERNLLSVAYKNVVGGQ
RAAWRVLSSIEQKSNEEGSEEKGPEVREYREKVETELQGVCDTVLGLLDSHLIKEAGDAE
SRVFYLKMKGDYYRYLAEVATGDDKKRIIDSARSAYQEAMDISKKEMPPTNPIRLGLALN
FSVFHYEIANSPEEAISLAKTTFDEAMADLHTLSEDSYKDSTLIMQLLRDNLTLWTADNA
GEEGGEAPQEPQS
Sequence of entity 2 (P), FASTA
>6Y3O_2 CAMKK2 (chains P)
RKLSLQER

Ligands and cofactors

IDNameFormulaCopies
MGMagnesium ionMg2
CACalcium ionCa1

Primary citation

A new soaking procedure for X-ray crystallographic structural determination of protein-peptide complexes. Ballone, A., Lau, R.A., Zweipfenning, F.P.A. et al. Acta Crystallogr F Struct Biol Commun (2020) 76:501-507. DOI 10.1107/S2053230X2001122X · 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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