PCSK9 CTD fragment structure. Determined by X-ray diffraction at 1.76 Å resolution. Released 27 May 2026.
Explore 9SZY in 3D Show helices and sheets RCSB PDB PDBe
9SZY contains 20 α-helices and 45 β-strands across 2 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 |
|---|---|---|---|
| β-strand | 63-65 | 3 | 1 |
| α-helix | 70-72 | 3 | |
| β-strand | 73-82 | 10 | 1 |
| α-helix | 88-103 | 16 | |
| β-strand | 110-115 | 6 | 1 |
| β-strand | 121-125 | 5 | 1 |
| α-helix | 128-130 | 3 | |
| α-helix | 131-135 | 5 | |
| β-strand | 140-147 | 8 | 1 |
| β-strand | 148-151 | 4 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 156-160 | 5 | |
| β-strand | 181-186 | 6 | 3 |
| β-strand | 200-206 | 7 | 3 |
| α-helix | 209-211 | 3 | |
| α-helix | 225-235 | 11 | |
| β-strand | 246-251 | 6 | 3 |
| β-strand | 258-260 | 3 | 2 |
| α-helix | 261-277 | 17 | |
| β-strand | 283-287 | 5 | 3 |
| β-strand | 289-292 | 4 | 2 |
| α-helix | 295-306 | 12 | |
| β-strand | 310-314 | 5 | 3 |
| β-strand | 318 | 1 | 4 |
| β-strand | 321 | 1 | 5 |
| α-helix | 322-324 | 3 | |
| β-strand | 325-326 | 2 | 2 |
| β-strand | 334-339 | 6 | 3 |
| α-helix | 344 | 1 | |
| β-strand | 345 | 1 | 3 |
| α-helix | 346 | 1 | |
| β-strand | 347-348 | 2 | 4 |
| β-strand | 351-352 | 2 | 4 |
| β-strand | 355 | 1 | 5 |
| β-strand | 361-364 | 4 | 3 |
| β-strand | 368-371 | 4 | 6 |
| β-strand | 379-382 | 4 | 6 |
| α-helix | 385-402 | 18 | |
| α-helix | 408-418 | 11 | |
| β-strand | 420-421 | 2 | 3 |
| α-helix | 426-428 | 3 | |
| α-helix | 431-434 | 4 | |
| β-strand | 440-441 | 2 | 3 |
| α-helix | 444-446 | 3 | |
| β-strand | 456-461 | 6 | 7 |
| α-helix | 462-464 | 3 | |
| β-strand | 472-475 | 4 | 8 |
| β-strand | 482-489 | 8 | 7 |
| β-strand | 495-496 | 2 | 8 |
| β-strand | 497 | 1 | 9 |
| β-strand | 498-502 | 5 | 8 |
| β-strand | 507-513 | 7 | 8 |
| α-helix | 514 | 1 | |
| β-strand | 521-528 | 8 | 7 |
| β-strand | 533-539 | 7 | 9 |
| β-strand | 548-551 | 4 | 10 |
| β-strand | 557-565 | 9 | 9 |
| β-strand | 587-590 | 4 | 10 |
| β-strand | 595-602 | 8 | 9 |
| β-strand | 606-615 | 10 | 11 |
| β-strand | 621-625 | 5 | 7 |
| α-helix | 626-627 | 2 | |
| β-strand | 631-637 | 7 | 11 |
| β-strand | 644-650 | 7 | 7 |
| β-strand | 653-658 | 6 | 7 |
| β-strand | 672-681 | 10 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Proprotein convertase subtilisin/kexin type 9 | A | protein | 152 | Homo sapiens | Q8NBP7 (AlphaFold model) |
| Proprotein convertase subtilisin/kexin type 9 | B | protein | 692 | Homo sapiens | Q8NBP7 (AlphaFold model) |
>9SZY_1 Proprotein convertase subtilisin/kexin type 9 (chains A) MGTVSSRRSWWPLPLLLLLLLLLGPAGARAQEDEDGDYEELVLALRSEEDGLAEAPEHGT TATFHRCAKDPWRLPGTYVVVLKEETHLSQSERTARRLQAQAARRGYLTKILHVFHGLLP GFLVKMSGDLLELALKLPHVDYIEEDSSVFAQ
>9SZY_2 Proprotein convertase subtilisin/kexin type 9 (chains B) MGTVSSRRSWWPLPLLLLLLLLLGPAGARAQEDEDGDYEELVLALRSEEDGLAEAPEHGT TATFHRCAKDPWRLPGTYVVVLKEETHLSQSERTARRLQAQAARRGYLTKILHVFHGLLP GFLVKMSGDLLELALKLPHVDYIEEDSSVFAQSIPWNLERITPPRYRADEYQPPDGGSLV EVYLLDTSIQSDHREIEGRVMVTDFENVPEEDGTRFHRQASKCDSHGTHLAGVVSGRDAG VAKGASMRSLRVLNCQGKGTVSGTLIGLEFIRKSQLVQPVGPLVVLLPLAGGYSRVLNAA CQRLARAGVVLVTAAGNFRDDACLYSPASAPEVITVGATNAQDQPVTLGTLGTNFGRCVD LFAPGEDIIGASSDCSTCFVSQSGTSQAAAHVAGIAAMMLSAEPELTLAELRQRLIHFSA KDVINEAWFPEDQRVLTPNLVAALPPSTHGAGWQLFCRTVWSAHSGPTRMATAIARCAPD EELLSCSSFSRSGKRRGERMEAQGGKLVCRAHNAFGGEGVYAIARCCLLPQANCSVHTAP PAEASMGTRVHCHQQGHVLTGCSSHWEVEDLGTHKPPVLRPRGQPNQCVGHREASIHASC CHAPGLECKVKEHGIPAPQEQVTVACEEGWTLTGCSALPGTSHVLGAYAVDNTCVVRSRD VSTTGSTSEGAVTAVAICCRSRHLAQASQELQ
| ID | Name | Formula | Copies |
|---|---|---|---|
| A1JSM | ~{N}-(2-methylpropyl)pyrimidin-2-amine | C8 H13 N3 | 1 |
Laroprovstat, the First Oral Small-Molecule PCSK9 Inhibitor for the Treatment of Hypercholesterolemia: Results From a Randomized, Single-Blind, Placebo-Controlled Phase 1 Trial in Treatment-Naive Patients. Vega, R.B., O'Mahony, G., Barbour, A.M. et al. Circulation (2026) 153:1999-2010. DOI 10.1161/CIRCULATIONAHA.125.075973 · PubMed
Other PDB entries of the same protein (UniProt Q8NBP7 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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