Two PLK1 PBD proteins bound to CENP-U(58-114) phosphorylated at Thr78 and Thr98. Determined by X-ray diffraction at 2.15 Å resolution. Released 24 Sept 2025.
Explore 9FJH in 3D Show helices and sheets RCSB PDB PDBe
9FJH contains 20 α-helices and 30 β-strands across 3 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 | 372-386 | 15 | |
| α-helix | 389-391 | 3 | |
| α-helix | 397-400 | 4 | |
| β-strand | 401 | 1 | 1 |
| α-helix | 403-405 | 3 | |
| β-strand | 411-417 | 7 | 2 |
| β-strand | 422-427 | 6 | 2 |
| β-strand | 432-436 | 5 | 2 |
| β-strand | 441-444 | 4 | 2 |
| β-strand | 450-454 | 5 | 2 |
| β-strand | 460-464 | 5 | 2 |
| α-helix | 470-472 | 3 | |
| α-helix | 473-489 | 17 | |
| β-strand | 490 | 1 | 3 |
| α-helix | 507-509 | 3 | |
| β-strand | 511-516 | 6 | 1 |
| β-strand | 520-525 | 6 | 1 |
| β-strand | 530-534 | 5 | 1 |
| β-strand | 540-544 | 5 | 1 |
| β-strand | 549-553 | 5 | 1 |
| β-strand | 559-563 | 5 | 1 |
| α-helix | 564-570 | 7 | |
| α-helix | 574-592 | 19 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 372-386 | 15 | |
| α-helix | 397-400 | 4 | |
| β-strand | 401 | 1 | 4 |
| α-helix | 403-405 | 3 | |
| β-strand | 411-417 | 7 | 5 |
| β-strand | 422-427 | 6 | 5 |
| β-strand | 432-436 | 5 | 5 |
| β-strand | 441-444 | 4 | 5 |
| β-strand | 450-454 | 5 | 5 |
| β-strand | 460-464 | 5 | 5 |
| α-helix | 470-472 | 3 | |
| α-helix | 473-489 | 17 | |
| α-helix | 507-509 | 3 | |
| β-strand | 511-516 | 6 | 4 |
| β-strand | 520-525 | 6 | 4 |
| β-strand | 530-534 | 5 | 4 |
| β-strand | 540-544 | 5 | 4 |
| β-strand | 549-553 | 5 | 4 |
| β-strand | 559-563 | 5 | 4 |
| α-helix | 564-570 | 7 | |
| α-helix | 574-594 | 21 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 75-76 | 2 | 2 |
| β-strand | 79 | 1 | 3 |
| α-helix | 80-82 | 3 | |
| α-helix | 84-93 | 10 | |
| β-strand | 96 | 1 | 5 |
| α-helix | 98-100 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Serine/threonine-protein kinase PLK1 | A, B | protein | 261 | Homo sapiens | P53350 (AlphaFold model) |
| Centromere protein U | C | protein | 59 | Homo sapiens | Q71F23 (AlphaFold model) |
>9FJH_1 Serine/threonine-protein kinase PLK1 (chains A, B) GSKGLENPLPERPREKEEPVVRETGEVVDCHLSDMLQQLHSVNASKPSERGLVRQEEAED PACIPIFWVSKWVDYSDKYGLGYQLCDNSVGVLFNDSTRLILYNDGDSLQYIERDGTESY LTVSSHPNSLMKKITLLKYFRNYMSEHLLKAGANITPREGDELARLPYLRTWFRTRSAII LHLSNGSVQINFFQDHTKLILCPLMAAVTYIDEKRDFRTYRLSLLEEYGCCKELASRLRY ARTMVDKLLSSRSASNRLKAS
>9FJH_2 Centromere protein U (chains C) GSLGENEKDEETYETFDPPLHSTAIYADEEEFSKHCGLSLSSTPPGKEAKRSSDTSGNE
| ID | Name | Formula | Copies |
|---|---|---|---|
| PO4 | Phosphate ion | O4 P | 1 |
Water and common crystallization additives (PGE, PG4) are not listed.
Structural and molecular basis of kinaseregulated inner-kinetochore recruitment of PLK1 by CENP-U. Ren, L., Gasper, R., Vetter, I.R. et al. To be published.
Other PDB entries of the same protein (UniProt P53350 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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