Structure of human alpha-2/delta-1 with crisugabalin. Determined by electron microscopy at 3.01 Å resolution. Released 7 Jan 2026.
Explore 9VLG in 3D Show helices and sheets RCSB PDB PDBe
9VLG contains 42 α-helices and 56 β-strands across 1 chain. 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 | 30-52 | 23 | |
| α-helix | 54-63 | 10 | |
| α-helix | 65-67 | 3 | |
| β-strand | 68-72 | 5 | 1 |
| α-helix | 75-109 | 35 | |
| α-helix | 118-120 | 3 | |
| β-strand | 126 | 1 | 2 |
| β-strand | 152 | 1 | 3 |
| β-strand | 155 | 1 | 3 |
| β-strand | 165-167 | 3 | 2 |
| α-helix | 177-186 | 10 | |
| α-helix | 189-199 | 11 | |
| β-strand | 207-210 | 4 | 2 |
| β-strand | 215-217 | 3 | 2 |
| α-helix | 242-248 | 7 | |
| β-strand | 253 | 1 | 4 |
| β-strand | 255-258 | 4 | 5 |
| α-helix | 268-282 | 15 | |
| β-strand | 288 | 1 | 4 |
| β-strand | 289 | 1 | 6 |
| β-strand | 291 | 1 | 5 |
| β-strand | 292-294 | 3 | 7 |
| β-strand | 298-300 | 3 | 7 |
| β-strand | 308 | 1 | 6 |
| α-helix | 312-323 | 12 | |
| α-helix | 333-344 | 12 | |
| β-strand | 357-361 | 5 | 5 |
| α-helix | 370-376 | 7 | |
| β-strand | 383-386 | 4 | 5 |
| β-strand | 389 | 1 | 8 |
| α-helix | 397-405 | 9 | |
| β-strand | 413 | 1 | 8 |
| α-helix | 416-419 | 4 | |
| α-helix | 426-430 | 5 | |
| α-helix | 432-437 | 6 | |
| β-strand | 450-451 | 2 | 9 |
| β-strand | 458-461 | 4 | 9 |
| β-strand | 464-466 | 3 | 2 |
| α-helix | 480-482 | 3 | |
| β-strand | 486-488 | 3 | 2 |
| β-strand | 491-493 | 3 | 9 |
| α-helix | 494-498 | 5 | |
| α-helix | 503-505 | 3 | |
| β-strand | 511-515 | 5 | 10 |
| β-strand | 520 | 1 | 11 |
| β-strand | 521 | 1 | 10 |
| α-helix | 536 | 1 | |
| β-strand | 537 | 1 | 9 |
| α-helix | 538 | 1 | |
| β-strand | 541 | 1 | 11 |
| α-helix | 542-545 | 4 | |
| α-helix | 550-558 | 9 | |
| β-strand | 565-567 | 3 | 10 |
| β-strand | 570-574 | 5 | 12 |
| β-strand | 581-585 | 5 | 12 |
| β-strand | 586-592 | 7 | 10 |
| β-strand | 599-605 | 7 | 10 |
| α-helix | 606-608 | 3 | |
| β-strand | 610-614 | 5 | 1 |
| α-helix | 638-640 | 3 | |
| α-helix | 641-644 | 4 | |
| β-strand | 646-649 | 4 | 13 |
| α-helix | 665-676 | 12 | |
| α-helix | 687-703 | 17 | |
| α-helix | 704-708 | 5 | |
| α-helix | 709-710 | 2 | |
| β-strand | 717-724 | 8 | 14 |
| β-strand | 728-731 | 4 | 13 |
| α-helix | 734-737 | 4 | |
| α-helix | 746-748 | 3 | |
| α-helix | 750-757 | 8 | |
| β-strand | 761 | 1 | 15 |
| β-strand | 762-764 | 3 | 14 |
| α-helix | 765-767 | 3 | |
| β-strand | 780-785 | 6 | 14 |
| β-strand | 788-789 | 2 | 16 |
| β-strand | 794-795 | 2 | 16 |
| β-strand | 798-804 | 7 | 14 |
| α-helix | 806-817 | 12 | |
| β-strand | 836-842 | 7 | 17 |
| β-strand | 846 | 1 | 18 |
| β-strand | 847-850 | 4 | 17 |
| β-strand | 862 | 1 | 18 |
| α-helix | 863-865 | 3 | |
| α-helix | 868-876 | 9 | |
| β-strand | 880-887 | 8 | 19 |
| β-strand | 964-971 | 8 | 19 |
| β-strand | 977-978 | 2 | 17 |
| β-strand | 991 | 1 | 17 |
| β-strand | 993-995 | 3 | 17 |
| α-helix | 996 | 1 | |
| β-strand | 999 | 1 | 15 |
| β-strand | 1001-1007 | 7 | 17 |
| α-helix | 1009-1011 | 3 | |
| α-helix | 1017-1020 | 4 | |
| β-strand | 1024 | 1 | 19 |
| α-helix | 1031-1034 | 4 | |
| α-helix | 1038-1040 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Isoform 2 of Voltage-dependent calcium channel subunit alpha-2/delta-1 | A | protein | 1064 | Homo sapiens | P54289 (AlphaFold model) |
>9VLG_1 Isoform 2 of Voltage-dependent calcium channel subunit alpha-2/delta-1 (chains A) HHHHHHHHWSHPQFEKEPFPSAVTIKSWVDKMQEDLVTLAKTASGVNQLVDIYEKYQDLY TVEPNNARQLVEIAARDIEKLLSNRSKALVRLALEAEKVQAAHQWREDFASNEVVYYNAK DDLDPEKNDSEPGSQRIKPVFIEDANFGRQISYQHAAVHIPTDIYEGSTIVLNELNWTSA LDEVFKKNREEDPSLLWQVFGSATGLARYYPASPWVDNSRTPNKIDLYDVRRRPWYIQGA ASPKDMLILVDVSGSVSGLTLKLIRTSVSEMLETLSDDDFVNVASFNSNAQDVSCFQHLV QANVRNKKVLKDAVNNITAKGITDYKKGFSFAFEQLLNYNVSRANCNKIIMLFTDGGEER AQEIFNKYNKDKKVRVFTFSVGQHNYDRGPIQWMACENKGYYYEIPSIGAIRINTQEYLD VLGRPMVLAGDKAKQVQWTNVYLDALELGLVITGTLPVFNITGQFENKTNLKNQLILGVM GVDVSLEDIKRLTPRFTLCPNGYYFAIDPNGYVLLHPNLQPKNPKSQEPVTLDFLDAELE NDIKVEIRNKMIDGESGEKTFRTLVKSQDERYIDKGNRTYTWTPVNGTDYSLALVLPTYS FYYIKAKLEETITQARSKKGKMKDSETLKPDNFEESGYTFIAPRDYCNDLKISDNNTEFL LNFNEFIDRHHHHHHHHKTPNNPSCNADLINRVLLDAGFTNELVQNYWSKQKNIKGVKAR FVVTDGGITRVYPKEAGENWQENPETYEDSFYKRSLDNDNYVFTAPYFNKSGPGAYESGI MVSKAVEIYIQGKLLKPAVVGIKIDVNSWIENFTKTSIRDPCAGPVCDCKRNSDVMDCVI LDDGGFLLMANHDDYTNQIGRFFGEIDPSLMRHLVNISVYAFNKSYDYQSVCEPGAAPKQ GAGHRSAYVPSVADILQIGWWATAAAWSILQQFLLSLTFPRLLEAVEMEDDDFTASLSKQ SCITEQTQYFFDNDSKSFSGVLDCGNCSRIFHGEKLMNTNLIFIMVESKGTCPCDTRLLI QAEQTSDGPNPCDMVKQPRYRKGPDVCFDNNVLEDYTDCGGVSG
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 2 |
| A1ESQ | Crisugabalin | C12 H19 N O2 | 1 |
Structural and Computational Insights into the Mechanism of the Superior Pharmacological Activity of Crisugabalin: A Third-Generation Cav alpha 2 delta 1 Ligand. Chen, Z., Gou, X., Meng, Q. et al. J Chem Inf Model (2026) 66:632-641. DOI 10.1021/acs.jcim.5c02583 · PubMed
Other PDB entries of the same protein (UniProt P54289 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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