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
| Element | Residues | Length | Sheet |
|---|
| α-helix | 4-16 | 13 | |
| α-helix | 20-32 | 13 | |
| α-helix | 36-37 | 2 | |
| α-helix | 39-70 | 32 | |
| α-helix | 76-103 | 28 | |
| α-helix | 104-108 | 5 | |
| α-helix | 117-135 | 19 | |
| α-helix | 140-164 | 25 | |
| α-helix | 170-181 | 12 | |
| α-helix | 182-187 | 6 | |
| α-helix | 190-206 | 17 | |
| α-helix | 208-210 | 3 | |
| α-helix | 216-240 | 25 | |
Chain B: 12 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 4-16 | 13 | |
| α-helix | 20-31 | 12 | |
| α-helix | 36-38 | 3 | |
| α-helix | 39-69 | 31 | |
| α-helix | 76-103 | 28 | |
| α-helix | 104-108 | 5 | |
| α-helix | 117-137 | 21 | |
| α-helix | 141-164 | 24 | |
| α-helix | 170-186 | 17 | |
| α-helix | 190-206 | 17 | |
| α-helix | 208-210 | 3 | |
| α-helix | 216-236 | 21 | |
Chain C: 13 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 4-16 | 13 | |
| α-helix | 20-31 | 12 | |
| α-helix | 39-69 | 31 | |
| α-helix | 70-73 | 4 | |
| α-helix | 76-103 | 28 | |
| α-helix | 104-108 | 5 | |
| α-helix | 117-137 | 21 | |
| α-helix | 140-164 | 25 | |
| α-helix | 170-181 | 12 | |
| α-helix | 182-186 | 5 | |
| α-helix | 190-205 | 16 | |
| α-helix | 208-210 | 3 | |
| α-helix | 216-236 | 21 | |
Chain D: 11 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 4-16 | 13 | |
| α-helix | 20-31 | 12 | |
| α-helix | 39-70 | 32 | |
| α-helix | 76-103 | 28 | |
| α-helix | 104-108 | 5 | |
| α-helix | 117-137 | 21 | |
| α-helix | 140-164 | 25 | |
| α-helix | 170-181 | 12 | |
| α-helix | 182-186 | 5 | |
| α-helix | 190-206 | 17 | |
| α-helix | 215-237 | 23 | |
Chain E: 13 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 4-16 | 13 | |
| α-helix | 20-31 | 12 | |
| α-helix | 36-38 | 3 | |
| α-helix | 39-73 | 35 | |
| α-helix | 76-103 | 28 | |
| α-helix | 104-108 | 5 | |
| α-helix | 109-111 | 3 | |
| α-helix | 117-135 | 19 | |
| α-helix | 141-164 | 24 | |
| α-helix | 170-185 | 16 | |
| α-helix | 190-206 | 17 | |
| α-helix | 216-234 | 19 | |
| α-helix | 235-237 | 3 | |
Chain F: 14 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 4-16 | 13 | |
| α-helix | 20-31 | 12 | |
| α-helix | 36-38 | 3 | |
| α-helix | 39-67 | 29 | |
| α-helix | 69-73 | 5 | |
| α-helix | 77-103 | 27 | |
| α-helix | 104-108 | 5 | |
| α-helix | 117-134 | 18 | |
| α-helix | 140-158 | 19 | |
| α-helix | 170-181 | 12 | |
| α-helix | 182-186 | 5 | |
| α-helix | 190-206 | 17 | |
| α-helix | 208-210 | 3 | |
| α-helix | 216-230 | 15 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| 14-3-3 protein gamma | A, B, C, D, E, F | protein | 240 | Homo sapiens | P61981 (AlphaFold model) |
| TSTTATPPVSQASSTTTSTW O-GlcNac peptide | G, P, T | protein | 20 | synthetic 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
| ID | Name | Formula | Copies |
|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 3 |
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:
- 6S9K 1.6 Å, Structure of 14-3-3 gamma in complex with caspase-2 peptide containing 14-3-3 binding…
- 6ZBT 1.8 Å, Structure of 14-3-3 gamma in complex with Nedd4-2 14-3-3 binding motif Ser342
- 3UZD 1.86 Å, Crystal structure of 14-3-3 GAMMA
- 6ZC9 1.9 Å, Structure of 14-3-3 gamma in complex with Nedd4-2 14-3-3 binding motif Ser448
- 6A5S 2.1 Å, Structure of 14-3-3 gamma in complex with TFEB 14-3-3 binding motif
- 4E2E 2.25 Å, Crystal structure of a tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation…
- 7A6Y 2.5 Å, Structure of 14-3-3 gamma in complex with DAPK2 peptide stabilized by FC-A
- 2B05 2.55 Å, Crystal Structure of 14-3-3 gamma in complex with a phosphoserine peptide
- 6GKF 2.6 Å, Structure of 14-3-3 gamma in complex with caspase-2 14-3-3 binding motif Ser139
- 6BZD 2.67 Å, Structure of 14-3-3 gamma R57E mutant bound to GlcNAcylated peptide
- 7A6R 2.7 Å, Structure of 14-3-3 gamma in complex with DAPK2 peptide containing the 14-3-3 binding…
- 5D3E 2.75 Å, Crystal structure of human 14-3-3 gamma in complex with CFTR R-domain peptide pS768-pS795
Browse structure collections
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