6BYJ: Human 14-3-3 gamma

Structure of human 14-3-3 gamma bound to O-GlcNAc peptide. Determined by X-ray diffraction at 2.9 Å resolution. Released 9 May 2018.

Method
X-ray diffraction
Resolution
2.9 Å
Organisms
Homo sapiens, synthetic construct
Chains
9
Atoms
11,720
Mol. weight
172.76 kDa
Ligands
NAG
Released
9 May 2018

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

Secondary structure: helices and β-sheets

6BYJ contains 76 α-helices and 0 β-strands across 6 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: 13 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix4-1613
α-helix20-3213
α-helix36-372
α-helix39-7032
α-helix76-10328
α-helix104-1085
α-helix117-13519
α-helix140-16425
α-helix170-18112
α-helix182-1876
α-helix190-20617
α-helix208-2103
α-helix216-24025
Chain B: 12 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix4-1613
α-helix20-3112
α-helix36-383
α-helix39-6931
α-helix76-10328
α-helix104-1085
α-helix117-13721
α-helix141-16424
α-helix170-18617
α-helix190-20617
α-helix208-2103
α-helix216-23621
Chain C: 13 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix4-1613
α-helix20-3112
α-helix39-6931
α-helix70-734
α-helix76-10328
α-helix104-1085
α-helix117-13721
α-helix140-16425
α-helix170-18112
α-helix182-1865
α-helix190-20516
α-helix208-2103
α-helix216-23621
Chain D: 11 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix4-1613
α-helix20-3112
α-helix39-7032
α-helix76-10328
α-helix104-1085
α-helix117-13721
α-helix140-16425
α-helix170-18112
α-helix182-1865
α-helix190-20617
α-helix215-23723
Chain E: 13 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix4-1613
α-helix20-3112
α-helix36-383
α-helix39-7335
α-helix76-10328
α-helix104-1085
α-helix109-1113
α-helix117-13519
α-helix141-16424
α-helix170-18516
α-helix190-20617
α-helix216-23419
α-helix235-2373
Chain F: 14 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix4-1613
α-helix20-3112
α-helix36-383
α-helix39-6729
α-helix69-735
α-helix77-10327
α-helix104-1085
α-helix117-13418
α-helix140-15819
α-helix170-18112
α-helix182-1865
α-helix190-20617
α-helix208-2103
α-helix216-23015

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
14-3-3 protein gammaA, B, C, D, E, Fprotein240Homo sapiensP61981 (AlphaFold model)
TSTTATPPVSQASSTTTSTW O-GlcNac peptideG, P, Tprotein20synthetic construct
Sequence of entity 1 (A, B, C, D, E, F), FASTA
>6BYJ_1 14-3-3 protein gamma (chains A, B, C, D, E, F)
VDREQLVQKARLAEQAERYDDMAAAMKNVTELNEPLSNEERNLLSVAYKNVVGARRSSWR
VISSIEQKTSADGNEKKIEMVRAYREKIEKELEAVCQDVLSLLDNYLIKNCSETQYESKV
FYLKMKGDYYRYLAEVATGEKRATVVESSEKAYSEAHEISKEHMQPTHPIRLGLALNYSV
FYYEIQNAPEQACHLAKTAFDDAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDQQDDD
Sequence of entity 2 (G, P, T), FASTA
>6BYJ_2 TSTTATPPVSQASSTTTSTW O-GlcNac peptide (chains G, P, T)
TSTTATPPVSQASSTTTSTW

Ligands and cofactors

IDNameFormulaCopies
NAG2-acetamido-2-deoxy-beta-D-glucopyranoseC8 H15 N O63

Primary citation

Structural basis of O-GlcNAc recognition by mammalian 14-3-3 proteins. Toleman, C.A., Schumacher, M.A., Yu, S.H. et al. Proc Natl Acad Sci U S A (2018) 115:5956-5961. DOI 10.1073/pnas.1722437115 · PubMed

Other PDB entries of the same protein (UniProt P61981 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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