4DAT: 14-3-3 sigma

Structure of 14-3-3 sigma in complex with PADI6 14-3-3 binding motif II. Determined by X-ray diffraction at 1.4 Å resolution. Released 13 Jun 2012.

Method
X-ray diffraction
Resolution
1.4 Å
Organism
Homo sapiens
Chains
2
Atoms
2,337
Mol. weight
27.46 kDa
Ligands
MG
Released
13 Jun 2012

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

Secondary structure: helices and β-sheets

4DAT 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-helix3-1513
α-helix19-3113
α-helix35-373
α-helix38-6629
α-helix80-10223
α-helix103-1075
α-helix108-1103
α-helix114-13421
α-helix141-16121
α-helix167-17812
α-helix179-1835
α-helix187-20216
α-helix205-2073
α-helix210-23021

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
14-3-3 protein sigmaAprotein234Homo sapiensP31947 (AlphaFold model)
Peptidylarginine Deiminase type VIBprotein9Homo sapiensQ6TGC4 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>4DAT_1 14-3-3 protein sigma (chains A)
MGSMERASLIQKAKLAEQAERYEDMAAFMKGAVEKGEELSCEERNLLSVAYKNVVGGQRA
AWRVLSSIEQKSNEEGSEEKGPEVREYREKVETELQGVCDTVLGLLDSHLIKEAGDAESR
VFYLKMKGDYYRYLAEVATGDDKKRIIDSARSAYQEAMDISKKEMPPTNPIRLGLALNFS
VFHYEIANSPEEAISLAKTTFDEAMADLHTLSEDSYKDSTLIMQLLRDNLTLWT
Sequence of entity 2 (B), FASTA
>4DAT_2 Peptidylarginine Deiminase type VI (chains B)
SSFYPSAEG

Ligands and cofactors

IDNameFormulaCopies
MGMagnesium ionMg1

Primary citation

Identification and structural characterization of two 14-3-3 binding sites in the human peptidylarginine deiminase type VI. Rose, R., Rose, M., Ottmann, C. J Struct Biol (2012) 180:65-72. DOI 10.1016/j.jsb.2012.05.010 · 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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