5D3E: Human 14-3-3 gamma
Crystal structure of human 14-3-3 gamma in complex with CFTR R-domain peptide pS768-pS795. Determined by X-ray diffraction at 2.75 Å resolution. Released 16 Mar 2016.
- Method
- X-ray diffraction
- Resolution
- 2.75 Å
- Organism
- Homo sapiens
- Chains
- 9
- Atoms
- 11,713
- Mol. weight
- 180.43 kDa
- Released
- 16 Mar 2016
Explore 5D3E in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
5D3E contains 79 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: 14 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 4-17 | 14 | |
| α-helix | 20-31 | 12 | |
| α-helix | 36-38 | 3 | |
| α-helix | 39-71 | 33 | |
| α-helix | 78-103 | 26 | |
| α-helix | 104-108 | 5 | |
| α-helix | 109-111 | 3 | |
| α-helix | 117-135 | 19 | |
| α-helix | 140-164 | 25 | |
| α-helix | 170-181 | 12 | |
| α-helix | 182-186 | 5 | |
| α-helix | 190-206 | 17 | |
| α-helix | 208-210 | 3 | |
| α-helix | 217-235 | 19 | |
Chain B: 14 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 4-16 | 13 | |
| α-helix | 20-32 | 13 | |
| α-helix | 35-38 | 4 | |
| α-helix | 39-73 | 35 | |
| α-helix | 76-103 | 28 | |
| α-helix | 104-108 | 5 | |
| α-helix | 109-111 | 3 | |
| 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 | 208-210 | 3 | |
| α-helix | 216-234 | 19 | |
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 | 39-69 | 31 | |
| α-helix | 76-103 | 28 | |
| α-helix | 104-108 | 5 | |
| α-helix | 117-136 | 20 | |
| α-helix | 140-164 | 25 | |
| α-helix | 170-181 | 12 | |
| α-helix | 182-186 | 5 | |
| α-helix | 190-206 | 17 | |
| α-helix | 208-210 | 3 | |
| α-helix | 216-234 | 19 | |
Chain F: 14 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | -1-1 | 3 | |
| α-helix | 4-16 | 13 | |
| α-helix | 20-32 | 13 | |
| α-helix | 36-38 | 3 | |
| α-helix | 39-69 | 31 | |
| 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 | 182-186 | 5 | |
| α-helix | 190-206 | 17 | |
| α-helix | 208-210 | 3 | |
| α-helix | 216-234 | 19 | |
Chain I: 12 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 4-17 | 14 | |
| α-helix | 20-33 | 14 | |
| α-helix | 39-73 | 35 | |
| 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 | 182-186 | 5 | |
| α-helix | 190-205 | 16 | |
| α-helix | 208-210 | 3 | |
| α-helix | 216-234 | 19 | |
Chain J: 12 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 4-16 | 13 | |
| α-helix | 20-31 | 12 | |
| α-helix | 39-73 | 35 | |
| α-helix | 77-79 | 3 | |
| α-helix | 80-103 | 24 | |
| α-helix | 104-108 | 5 | |
| α-helix | 118-134 | 17 | |
| α-helix | 141-164 | 24 | |
| α-helix | 170-181 | 12 | |
| α-helix | 182-186 | 5 | |
| α-helix | 190-205 | 16 | |
| α-helix | 219-233 | 15 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| 14-3-3 protein gamma | A, B, E, F, I, J | protein | 241 | Homo sapiens | P61981 (AlphaFold model) |
| Cystic fibrosis transmembrane conductance regulator | C, G, K | protein | 40 | Homo sapiens | P13569 (AlphaFold model) |
Sequence of entity 1 (A, B, E, F, I, J), FASTA
>5D3E_1 14-3-3 protein gamma (chains A, B, E, F, I, J)
MGSMVDREQLVQKARLAEQAERYDDMAAAMKNVTELNEPLSNEERNLLSVAYKNVVGARR
SSWRVISSIEQKTSADGNEKKIEMVRAYREKIEKELEAVCQDVLSLLDNYLIKNCSETQY
ESKVFYLKMKGDYYRYLAEVATGEKRATVVESSEKAYSEAHEISKEHMQPTHPIRLGLAL
NYSVFYYEIQNAPEQACHLAKTAFDDAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDQ
Q
Sequence of entity 2 (C, G, K), FASTA
>5D3E_2 Cystic fibrosis transmembrane conductance regulator (chains C, G, K)
QARRRQSVLNLMTHSVNQGQNIHRKTTASTRKVSLAPQAN
Primary citation
Characterization and small-molecule stabilization of the multisite tandem binding between 14-3-3 and the R domain of CFTR. Stevers, L.M., Lam, C.V., Leysen, S.F. et al. Proc Natl Acad Sci U S A (2016) 113:E1152-E1161. DOI 10.1073/pnas.1516631113 · 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…
- 6SAD 2.75 Å, Structure of 14-3-3 gamma in complex with double phosphorylated caspase-2 peptide on…
Browse structure collections
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