NG domain of human SRP54 T117 deletion mutant. Determined by X-ray diffraction at 4.0 Å resolution. Released 23 Sept 2020.
Explore 6Y31 in 3D Show helices and sheets RCSB PDB PDBe
6Y31 contains 55 α-helices and 32 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 | 4-18 | 15 | |
| α-helix | 25-41 | 17 | |
| α-helix | 46-59 | 14 | |
| α-helix | 71-87 | 17 | |
| α-helix | 92-94 | 3 | |
| β-strand | 102-108 | 7 | 1 |
| α-helix | 118-127 | 10 | |
| β-strand | 132-135 | 4 | 1 |
| α-helix | 148-155 | 8 | |
| β-strand | 159 | 1 | 1 |
| α-helix | 168-181 | 14 | |
| β-strand | 186-190 | 5 | 1 |
| α-helix | 198-212 | 15 | |
| β-strand | 216-222 | 7 | 1 |
| α-helix | 223-228 | 6 | |
| α-helix | 229-237 | 9 | |
| β-strand | 243-248 | 6 | 1 |
| α-helix | 256-265 | 10 | |
| α-helix | 268-269 | 2 | |
| β-strand | 270-274 | 5 | 1 |
| β-strand | 282-284 | 3 | 1 |
| α-helix | 287-295 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-19 | 16 | |
| α-helix | 25-41 | 17 | |
| α-helix | 46-59 | 14 | |
| α-helix | 71-87 | 17 | |
| α-helix | 92-94 | 3 | |
| β-strand | 102-108 | 7 | 2 |
| α-helix | 116-127 | 11 | |
| β-strand | 132-136 | 5 | 2 |
| α-helix | 143-155 | 13 | |
| β-strand | 159-161 | 3 | 2 |
| α-helix | 168-181 | 14 | |
| β-strand | 186-190 | 5 | 2 |
| α-helix | 198-212 | 15 | |
| β-strand | 216-222 | 7 | 2 |
| α-helix | 223-228 | 6 | |
| α-helix | 229-239 | 11 | |
| β-strand | 243-248 | 6 | 2 |
| α-helix | 256-265 | 10 | |
| β-strand | 270-274 | 5 | 2 |
| β-strand | 282-284 | 3 | 2 |
| α-helix | 287-295 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-18 | 15 | |
| α-helix | 25-41 | 17 | |
| α-helix | 46-59 | 14 | |
| α-helix | 71-87 | 17 | |
| α-helix | 92-94 | 3 | |
| β-strand | 102-108 | 7 | 3 |
| α-helix | 116-127 | 11 | |
| β-strand | 132-136 | 5 | 3 |
| α-helix | 143-154 | 12 | |
| β-strand | 159-160 | 2 | 3 |
| α-helix | 168-181 | 14 | |
| β-strand | 186-190 | 5 | 3 |
| α-helix | 198-212 | 15 | |
| β-strand | 216-222 | 7 | 3 |
| α-helix | 223-228 | 6 | |
| α-helix | 229-237 | 9 | |
| β-strand | 243-248 | 6 | 3 |
| α-helix | 256-265 | 10 | |
| α-helix | 268-269 | 2 | |
| β-strand | 270-274 | 5 | 3 |
| β-strand | 282-284 | 3 | 3 |
| α-helix | 287-295 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-18 | 15 | |
| α-helix | 25-41 | 17 | |
| α-helix | 46-59 | 14 | |
| α-helix | 71-87 | 17 | |
| α-helix | 92-94 | 3 | |
| β-strand | 102-108 | 7 | 4 |
| α-helix | 116-127 | 11 | |
| β-strand | 132-136 | 5 | 4 |
| α-helix | 143-155 | 13 | |
| β-strand | 159-160 | 2 | 4 |
| α-helix | 168-181 | 14 | |
| β-strand | 186-190 | 5 | 4 |
| α-helix | 198-212 | 15 | |
| β-strand | 216-222 | 7 | 4 |
| α-helix | 223-228 | 6 | |
| α-helix | 229-237 | 9 | |
| β-strand | 243-248 | 6 | 4 |
| α-helix | 256-265 | 10 | |
| α-helix | 268-269 | 2 | |
| β-strand | 270-274 | 5 | 4 |
| β-strand | 282-284 | 3 | 4 |
| α-helix | 287-295 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Signal recognition particle 54 kDa protein | A, B, C, D | protein | 303 | Homo sapiens | P61011 (AlphaFold model) |
>6Y31_1 Signal recognition particle 54 kDa protein (chains A, B, C, D) MGHHHHHHMVLADLGRKITSALRSLSNATIINEEVLNAMLKEVCTALLEADVNIKLVKQL RENVKSAIDLEEMASGLNKRKMIQHAVFKELVKLVDPGVKAWTPTKGKQNVIMFVGLQGS GKTTCSKLAYYYQRKGWKTCLICADTFRAGAFDQLKQNATKARIPFYGSYTEMDPVIIAS EGVEKFKNENFEIIIVDTSGRHKQEDSLFEEMLQVANAIQPDNIVYVMDASIGQACEAQA KAFKDKVDVASVIVTKLDGHAKGGGALSAVAATKSPIIFIGTGEHIDDFEPFKTQPFISK LLG
Structural and Functional Impact of SRP54 Mutations Causing Severe Congenital Neutropenia. Juaire, K.D., Lapouge, K., Becker, M.M.M. et al. Structure (2021) 29:15. DOI 10.1016/j.str.2020.09.008 · PubMed
Other PDB entries of the same protein (UniProt P61011 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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