RepoMan-PP1a (protein phosphatase 1, alpha isoform) holoenzyme complex. Determined by X-ray diffraction at 2.57 Å resolution. Released 5 Oct 2016.
Explore 5IOH in 3D Show helices and sheets RCSB PDB PDBe
5IOH contains 30 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 | 18-20 | 3 | |
| α-helix | 23 | 1 | |
| 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 | 184-187 | 4 | |
| 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 | 229-238 | 10 | |
| 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 | |
| α-helix | 278-279 | 2 | |
| β-strand | 280-285 | 6 | 2 |
| β-strand | 290-298 | 9 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 394-395 | 2 | 2 |
| β-strand | 402-404 | 3 | 2 |
| β-strand | 415 | 1 | 2 |
| α-helix | 416-418 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 9-17 | 9 | |
| α-helix | 18-20 | 3 | |
| α-helix | 23 | 1 | |
| α-helix | 32-48 | 17 | |
| β-strand | 52-55 | 4 | 5 |
| 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 | 128-131 | 4 | |
| α-helix | 136-143 | 8 | |
| α-helix | 146-156 | 11 | |
| β-strand | 162-165 | 4 | 5 |
| β-strand | 169-171 | 3 | 5 |
| α-helix | 184-187 | 4 | |
| α-helix | 200-206 | 7 | |
| β-strand | 209 | 1 | 8 |
| β-strand | 216 | 1 | 8 |
| β-strand | 227 | 1 | 8 |
| α-helix | 229-238 | 10 | |
| 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 | |
| α-helix | 278-279 | 2 | |
| β-strand | 280-285 | 6 | 6 |
| β-strand | 290-298 | 9 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Serine/threonine-protein phosphatase PP1-alpha catalytic subunit | A, C | protein | 299 | Homo sapiens | P62136 (AlphaFold model) |
| Cell division cycle-associated protein 2 | B, D | protein | 64 | Homo sapiens | Q69YH5 (AlphaFold model) |
>5IOH_1 Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (chains A, C) GHMGSLNLDSIIGRLLEVQGSRPGKNVQLTENEIRGLCLKSREIFLSQPILLELEAPLKI CGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLL RGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQ SMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGAEVVAKFLHKHDL DLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPAD
>5IOH_2 Cell division cycle-associated protein 2 (chains B, D) GAMGYAFLNMRKRKRVTFGEDLSPEVFDESLPANTPLRKGGTPVCKKDFSGLSSLLLEQS PVPE
The Ki-67 and RepoMan mitotic phosphatases assemble via an identical, yet novel mechanism. Kumar, G.S., Gokhan, E., De Munter, S. et al. Elife (2016) 5. DOI 10.7554/eLife.16539 · 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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