Cryo-EM structure of human SV2A in complex with Brivaracetam. Determined by electron microscopy at 3.38 Å resolution. Released 12 Jun 2024.
Explore 8YF1 in 3D Show helices and sheets RCSB PDB PDBe
8YF1 contains 56 α-helices and 16 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 |
|---|---|---|---|
| α-helix | 134-159 | 26 | |
| α-helix | 163-188 | 26 | |
| α-helix | 193-195 | 3 | |
| α-helix | 203-229 | 27 | |
| α-helix | 231-250 | 20 | |
| α-helix | 255-270 | 16 | |
| α-helix | 273-280 | 8 | |
| α-helix | 281-283 | 3 | |
| α-helix | 286-293 | 8 | |
| α-helix | 294-296 | 3 | |
| α-helix | 297-314 | 18 | |
| α-helix | 332-340 | 9 | |
| α-helix | 342-351 | 10 | |
| α-helix | 355-357 | 3 | |
| α-helix | 358-363 | 6 | |
| α-helix | 368-382 | 15 | |
| α-helix | 387-390 | 4 | |
| α-helix | 393-401 | 9 | |
| α-helix | 420-437 | 18 | |
| α-helix | 446-462 | 17 | |
| α-helix | 463-467 | 5 | |
| α-helix | 468-482 | 15 | |
| β-strand | 486 | 1 | 4 |
| β-strand | 505 | 1 | 4 |
| β-strand | 507 | 1 | 5 |
| β-strand | 521-522 | 2 | 6 |
| β-strand | 527 | 1 | 5 |
| β-strand | 530 | 1 | 7 |
| β-strand | 541-542 | 2 | 6 |
| β-strand | 547 | 1 | 5 |
| β-strand | 550 | 1 | 7 |
| α-helix | 592-594 | 3 | |
| α-helix | 595-619 | 25 | |
| α-helix | 627-642 | 16 | |
| α-helix | 649-676 | 28 | |
| α-helix | 682-706 | 25 | |
| α-helix | 714-726 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 134-159 | 26 | |
| α-helix | 164-184 | 21 | |
| α-helix | 185-189 | 5 | |
| α-helix | 203-225 | 23 | |
| α-helix | 232-250 | 19 | |
| α-helix | 255-270 | 16 | |
| α-helix | 273-281 | 9 | |
| α-helix | 290-293 | 4 | |
| α-helix | 296-314 | 19 | |
| α-helix | 319-321 | 3 | |
| α-helix | 333-340 | 8 | |
| α-helix | 342-350 | 9 | |
| α-helix | 355-357 | 3 | |
| α-helix | 358-364 | 7 | |
| α-helix | 368-381 | 14 | |
| α-helix | 389-398 | 10 | |
| α-helix | 416-438 | 23 | |
| α-helix | 444-456 | 13 | |
| α-helix | 459-462 | 4 | |
| α-helix | 463-467 | 5 | |
| α-helix | 468-483 | 16 | |
| β-strand | 504 | 1 | 1 |
| β-strand | 524 | 1 | 1 |
| β-strand | 532 | 1 | 2 |
| β-strand | 535-536 | 2 | 3 |
| β-strand | 552 | 1 | 2 |
| β-strand | 555-556 | 2 | 3 |
| α-helix | 563-565 | 3 | |
| β-strand | 575 | 1 | 3 |
| α-helix | 597-608 | 12 | |
| α-helix | 610-621 | 12 | |
| α-helix | 626-643 | 18 | |
| α-helix | 650-676 | 27 | |
| α-helix | 679-681 | 3 | |
| α-helix | 682-707 | 26 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Synaptic vesicle glycoprotein 2A | A, B | protein | 755 | Homo sapiens | Q7L0J3 (AlphaFold model) |
>8YF1_1 Synaptic vesicle glycoprotein 2A (chains A, B) MEEGFRDRAAFIRGAKDIAKEVKKHAAKKVVKGLDRVQDEYSRRSYSRFEEEDDDDDFPA PSDGYYRGEGTQDEEEGGASSDATEGHDEDDEIYEGEYQGIPRAESGGKGERMADGAPLA GVRGGLSDGEGPPGGRGEAQRRKEREELAQQYEAILRECGHGRFQWTLYFVLGLALMADG VEVFVVGFVLPSAEKDMCLSDSNKGMLGLIVYLGMMVGAFLWGGLADRLGRRQCLLISLS VNSVFAFFSSFVQGYGTFLFCRLLSGVGIGGSIPIVFSYFSEFLAQEKRGEHLSWLCMFW MIGGVYAAAMAWAIIPHYGWSFQMGSAYQFHSWRVFVLVCAFPSVFAIGALTTQPESPRF FLENGKHDEAWMVLKQVHDTNMRAKGHPERVFSVTHIKTIHQEDELIEIQSDTGTWYQRW GVRALSLGGQVWGNFLSCFGPEYRRITLMMMGVWFTMSFSYYGLTVWFPDMIRHLQAVDY ASRTKVFPGERVEHVTFNFTLENQIHRGGQYFNDKFIGLRLKSVSFEDSLFEECYFEDVT SSNTFFRNCTFINTVFYNTDLFEYKFVNSRLINSTFLHNKEGCPLDVTGTGEGAYMVYFV SFLGTLAVLPGNIVSALLMDKIGRLRMLAGSSVMSCVSCFFLSFGNSESAMIALLCLFGG VSIASWNALDVLTVELYPSDKRTTAFGFLNALCKLAAVLGISIFTSFVGITKAAPILFAS AALALGSSLALKLPSRLEEELRRRTEPGSLEVLFQ
| ID | Name | Formula | Copies |
|---|---|---|---|
| VLX | (2S)-2-[(4R)-2-oxidanylidene-4-propyl-pyrrolidin-1-yl]butanamide | C11 H20 N2 O2 | 2 |
Recognition of antiepileptic brivaracetam by synaptic vesicle protein 2A. Liu, S., Chao, Y., Zhou, Z. et al. Cell Discov (2024) 10:56-56. DOI 10.1038/s41421-024-00686-9 · 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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