Pathogenic mutations of human phosphorylation sites affect protein-protein interactions. Determined by X-ray diffraction at 3.23 Å resolution. Released 21 Feb 2024.
Explore 8Q1S in 3D Show helices and sheets RCSB PDB PDBe
8Q1S contains 27 α-helices and 0 β-strands across 4 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-16 | 14 | |
| α-helix | 20-32 | 13 | |
| 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 | 115-135 | 21 | |
| α-helix | 138-161 | 24 | |
| α-helix | 168-183 | 16 | |
| α-helix | 188-203 | 16 | |
| α-helix | 214-231 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-16 | 14 | |
| α-helix | 20-32 | 13 | |
| 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 | 115-135 | 21 | |
| α-helix | 139-162 | 24 | |
| α-helix | 168-183 | 16 | |
| α-helix | 188-204 | 17 | |
| α-helix | 206-208 | 3 | |
| α-helix | 211-234 | 24 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 102-105 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 101-103 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| 14-3-3 protein epsilon | A, B | protein | 255 | Homo sapiens | P62258 (AlphaFold model) |
| GATA zinc finger domain-containing protein 1 | C, P | protein | 15 | Homo sapiens | Q8WUU5 (AlphaFold model) |
>8Q1S_1 14-3-3 protein epsilon (chains A, B) MDDREDLVYQAKLAEQAERYDEMVESMKKVAGMDVELTVEERNLLSVAYKNVIGARRASW RIISSIEQKEENKGGEDKLKMIREYRQMVETELKLICCDILDVLDKHLIPAANTGESKVF YYKMKGDYHRYLAEFATGNDRKEAAENSLVAYKAASDIAMTELPPTHPIRLGLALNFSVF YYEILNSPDRACRLAKAAFDDAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSDMQGDGE EQNKEALQDVEDENQ
>8Q1S_2 GATA zinc finger domain-containing protein 1 (chains C, P) LRNTKYKSAPAAEKK
Pathogenic mutations of human phosphorylation sites affect protein-protein interactions. Rrustemi, T., Meyer, K., Roske, Y. et al. Nat Commun (2024) 15:3146-3146. DOI 10.1038/s41467-024-46794-8 · PubMed
Other PDB entries of the same protein (UniProt P62258 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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