The Ribosomal RNA Processing 1B Protein Phosphatase-1 Holoenzyme. Determined by X-ray diffraction at 1.8 Å resolution. Released 7 Dec 2022.
Explore 7T0Y in 3D Show helices and sheets RCSB PDB PDBe
7T0Y contains 35 α-helices and 38 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 | 9-17 | 9 | |
| α-helix | 18-21 | 4 | |
| α-helix | 32-48 | 17 | |
| β-strand | 52-55 | 4 | 1 |
| β-strand | 59-62 | 4 | 2 |
| β-strand | 64 | 1 | 3 |
| α-helix | 69-79 | 11 | |
| β-strand | 87-89 | 3 | 2 |
| α-helix | 100-113 | 14 | |
| β-strand | 118-120 | 3 | 2 |
| α-helix | 128-131 | 4 | |
| α-helix | 136-143 | 8 | |
| α-helix | 146-156 | 11 | |
| β-strand | 162-165 | 4 | 1 |
| β-strand | 169-171 | 3 | 1 |
| α-helix | 183-187 | 5 | |
| α-helix | 194-196 | 3 | |
| α-helix | 200-206 | 7 | |
| β-strand | 208-209 | 2 | 4 |
| β-strand | 216-218 | 3 | 4 |
| β-strand | 225-227 | 3 | 4 |
| α-helix | 229-239 | 11 | |
| β-strand | 243-246 | 4 | 1 |
| β-strand | 255-258 | 4 | 1 |
| β-strand | 263-266 | 4 | 1 |
| β-strand | 267 | 1 | 3 |
| α-helix | 272-274 | 3 | |
| β-strand | 280-285 | 6 | 2 |
| β-strand | 290-298 | 9 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 685-686 | 2 | 2 |
| α-helix | 688-690 | 3 | |
| β-strand | 692-696 | 5 | 2 |
| α-helix | 702-705 | 4 | |
| α-helix | 719-721 | 3 | |
| β-strand | 726 | 1 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 9-17 | 9 | |
| α-helix | 18-21 | 4 | |
| α-helix | 23 | 1 | |
| α-helix | 32-48 | 17 | |
| β-strand | 52-55 | 4 | 5 |
| α-helix | 56 | 1 | |
| α-helix | 58 | 1 | |
| β-strand | 59-62 | 4 | 6 |
| β-strand | 64 | 1 | 7 |
| α-helix | 69-79 | 11 | |
| β-strand | 87-89 | 3 | 6 |
| α-helix | 100-113 | 14 | |
| β-strand | 118-120 | 3 | 6 |
| α-helix | 121-123 | 3 | |
| α-helix | 128-134 | 7 | |
| α-helix | 136-143 | 8 | |
| α-helix | 146-156 | 11 | |
| β-strand | 162-165 | 4 | 5 |
| β-strand | 169-172 | 4 | 5 |
| α-helix | 183-187 | 5 | |
| α-helix | 194-196 | 3 | |
| α-helix | 200-206 | 7 | |
| β-strand | 208-209 | 2 | 8 |
| β-strand | 216-218 | 3 | 8 |
| β-strand | 225-227 | 3 | 8 |
| α-helix | 229-239 | 11 | |
| β-strand | 243-246 | 4 | 5 |
| β-strand | 255-258 | 4 | 5 |
| β-strand | 263-266 | 4 | 5 |
| β-strand | 267 | 1 | 7 |
| α-helix | 272-274 | 3 | |
| β-strand | 280-285 | 6 | 6 |
| β-strand | 290-298 | 9 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 685-686 | 2 | 6 |
| α-helix | 688-690 | 3 | |
| β-strand | 692-696 | 5 | 6 |
| α-helix | 702-704 | 3 | |
| β-strand | 726 | 1 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Serine/threonine-protein phosphatase PP1-alpha catalytic subunit | A, C | protein | 299 | Homo sapiens | P62136 (AlphaFold model) |
| Ribosomal RNA processing protein 1 homolog B | B, D | protein | 47 | Homo sapiens | Q14684 (AlphaFold model) |
>7T0Y_1 Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (chains A, C) GHMGSLNLDSIIGRLLEVRGSRPGKNVQLTENEIRGLCLKSREIFLSQPILLELEAPLKI CGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLL RGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQ SMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGAEVVAKFLHKHDL DLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPAD
>7T0Y_2 Ribosomal RNA processing protein 1 homolog B (chains B, D) GKKVTFGLNRNMTAEFKKTDKSILVSPTGPSRVAFDPEQKPLHGVLK
Water and common crystallization additives (BR, EDO) are not listed.
The ribosomal RNA processing 1B:protein phosphatase 1 holoenzyme reveals non-canonical PP1 interaction motifs. Srivastava, G., Bajaj, R., Kumar, G.S. et al. Cell Rep (2022) 41:111726-111726. DOI 10.1016/j.celrep.2022.111726 · PubMed
Other PDB entries of the same protein (UniProt P62136 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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