Cryo-EM structure of human SV2A in complex with UCBJ. Determined by electron microscopy at 2.39 Å resolution. Released 10 Dec 2025.
Explore 9OKH in 3D Show helices and sheets RCSB PDB PDBe
9OKH contains 26 α-helices and 0 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 | 140-159 | 20 | |
| α-helix | 163-184 | 22 | |
| α-helix | 185-189 | 5 | |
| α-helix | 201-229 | 29 | |
| α-helix | 231-249 | 19 | |
| α-helix | 255-269 | 15 | |
| α-helix | 272-281 | 10 | |
| α-helix | 289-295 | 7 | |
| α-helix | 298-314 | 17 | |
| α-helix | 318-320 | 3 | |
| α-helix | 332-340 | 9 | |
| α-helix | 342-351 | 10 | |
| α-helix | 355-357 | 3 | |
| α-helix | 358-363 | 6 | |
| α-helix | 367-385 | 19 | |
| α-helix | 416-436 | 21 | |
| α-helix | 437-439 | 3 | |
| α-helix | 444-478 | 35 | |
| α-helix | 594-606 | 13 | |
| α-helix | 608-622 | 15 | |
| α-helix | 624-641 | 18 | |
| α-helix | 642-644 | 3 | |
| α-helix | 648-675 | 28 | |
| α-helix | 682-706 | 25 | |
| α-helix | 713-730 | 18 | |
| α-helix | 734-735 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Synaptic vesicle glycoprotein 2A | A | protein | 604 | Homo sapiens | Q7L0J3 (AlphaFold model) |
>9OKH_1 Synaptic vesicle glycoprotein 2A (chains A) AQRRKEREELAQQYEAILRECGHGRFQWTLYFVLGLALMADGVEVFVVGFVLPSAEKDMC LSDSNKGMLGLIVYLGMMVGAFLWGGLADRLGRRQCLLISLSVNSVFAFFSSFVQGYGTF LFCRLLSGVGIGGSIPIVFSYFSEFLAQEKRGEHLSWLCMFWMIGGVYAAAMAWAIIPHY GWSFQMGSAYQFHSWRVFVLVCAFPSVFAIGALTTQPESPRFFLENGKHDEAWMVLKQVH DTNMRAKGHPERVFSVTHIKTIHQEDELIEIQSDTGTWYQRWGVRALSLGGQVWGNFLSC FGPEYRRITLMMMGVWFTMSFSYYGLTVWFPDMIRHLQAVDYASRTKVFPGERVEHVTFN FTLENQIHRGGQYFNDKFIGLRLKSVSFEDSLFEECYFEDVTSSNTFFRNCTFINTVFYN TDLFEYKFVNSRLINSTFLHNKEGCPLDVTGTGEGAYMVYFVSFLGTLAVLPGNIVSALL MDKIGRLRMLAGSSVMSCVSCFFLSFGNSESAMIALLCLFGGVSIASWNALDVLTVELYP SDKRTTAFGFLNALCKLAAVLGISIFTSFVGITKAAPILFASAALALGSSLALKLPETRG QVLQ
| ID | Name | Formula | Copies |
|---|---|---|---|
| A1CCA | (4R)-1-[(3-methylpyridin-4-yl)methyl]-4-(3,4,5-trifluorophenyl)pyrrolidin-2-one | C17 H15 F3 N2 O | 1 |
Structural pharmacology of SV2A reveals an allosteric modulation mechanism in the major facilitator superfamily. Pidathala, S., Chen, X., Dai, Y. et al. Nat Commun (2025) 16:10748-10748. DOI 10.1038/s41467-025-65781-1 · PubMed
Other PDB entries of the same protein (UniProt Q7L0J3 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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