Structure of Synaptic Vesicle Protein 2A Bound to Brivaracetam and UCB1244283. Determined by electron microscopy at 3.05 Å resolution. Released 10 Sept 2025.
Explore 9NTC in 3D Show helices and sheets RCSB PDB PDBe
9NTC contains 23 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 | 143-159 | 17 | |
| α-helix | 164-188 | 25 | |
| α-helix | 207-209 | 3 | |
| α-helix | 210-229 | 20 | |
| α-helix | 231-248 | 18 | |
| α-helix | 258-270 | 13 | |
| α-helix | 272-280 | 9 | |
| α-helix | 281-283 | 3 | |
| α-helix | 286-294 | 9 | |
| α-helix | 297-314 | 18 | |
| α-helix | 333-339 | 7 | |
| α-helix | 342-351 | 10 | |
| α-helix | 355-357 | 3 | |
| α-helix | 358-363 | 6 | |
| α-helix | 368-383 | 16 | |
| α-helix | 426-437 | 12 | |
| α-helix | 444-482 | 39 | |
| α-helix | 594-622 | 29 | |
| α-helix | 624-641 | 18 | |
| α-helix | 642-644 | 3 | |
| α-helix | 648-675 | 28 | |
| α-helix | 682-706 | 25 | |
| α-helix | 714-730 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Synaptic vesicle glycoprotein 2A | A | protein | 686 | Homo sapiens | Q7L0J3 (AlphaFold model) |
>9NTC_1 Synaptic vesicle glycoprotein 2A (chains A) MGYYRGEGTQDEEEGGASSDATEGHDEDDEIYEGEYQGIPRAESGGKGERMADGAPLAGV RGGLSDGEGPPGGRGEAQRRKEREELAQQYEAILRECGHGRFQWTLYFVLGLALMADGVE VFVVGFVLPSAEKDMCLSDSNKGMLGLIVYLGMMVGAFLWGGLADRLGRRQCLLISLSVN SVFAFFSSFVQGYGTFLFCRLLSGVGIGGSIPIVFSYFSEFLAQEKRGEHLSWLCMFWMI GGVYAAAMAWAIIPHYGWSFQMGSAYQFHSWRVFVLVCAFPSVFAIGALTTQPESPRFFL ENGKHDEAWMVLKQVHDTNMRAKGHPERVFSVTHIKTIHQEDELIEIQSDTGTWYQRWGV RALSLGGQVWGNFLSCFGPEYRRITLMMMGVWFTMSFSYYGLTVWFPDMIRHLQAVDYAS RTKVFPGERVEHVTFNFTLENQIHRGGQYFNDKFIGLRLKSVSFEDSLFEECYFEDVTSS NTFFRNCTFINTVFYNTDLFEYKFVNSRLINSTFLHNKEGCPLDVTGTGEGAYMVYFVSF LGTLAVLPGNIVSALLMDKIGRLRMLAGSSVMSCVSCFFLSFGNSESAMIALLCLFGGVS IASWNALDVLTVELYPSDKRTTAFGFLNALCKLAAVLGISIFTSFVGITKAAPILFASAA LALGSSLALKLPETRGQVLQLEVLFQ
| ID | Name | Formula | Copies |
|---|---|---|---|
| A1B1J | (3R)-4-(3,5-dimethylphenyl)-N-(2-methoxyphenyl)-3-methylbutanamide | C20 H25 N O2 | 1 |
| VLX | (2S)-2-[(4R)-2-oxidanylidene-4-propyl-pyrrolidin-1-yl]butanamide | C11 H20 N2 O2 | 1 |
| CLR | Cholesterol | C27 H46 O | 1 |
| A1B1I | (3S)-4-(3,5-dimethylphenyl)-N-(2-methoxyphenyl)-3-methylbutanamide | C20 H25 N O2 | 1 |
Mechanisms underlying allosteric modulation of antiseizure medication binding to synaptic vesicle protein 2A (SV2A). Mittal, A., Martin, M.F., Provins, L. et al. Proc Natl Acad Sci U S A (2025) 122:e2510239122-e2510239122. DOI 10.1073/pnas.2510239122 · 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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