9PFG: Synaptosomal-associated protein 25
Min22bin20S complex (NSF-alphaSNAP-2:2 syntaxin-1a H3:SNAP-25 SN1), 4:2:2 alphaSNAP-syntaxin-1a H3-SNAP-25 SN1 subcomplex local refinement, non-hydrolyzing, class 28. Determined by electron microscopy at 3.58 Å resolution. Released 6 Aug 2025.
- Method
- Electron microscopy
- Resolution
- 3.58 Å
- Organisms
- Rattus norvegicus, Cricetulus griseus
- Chains
- 10
- Atoms
- 13,908
- Mol. weight
- 336.93 kDa
- Released
- 6 Aug 2025
Explore 9PFG in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
9PFG contains 81 α-helices and 30 β-strands across 10 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.
Chain A: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 20-82 | 63 | |
Chains B and D: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 192-257 | 66 | |
Chain C: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 20-81 | 62 | |
Chain E: 16 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-23 | 21 | |
| α-helix | 36-54 | 19 | |
| α-helix | 58-74 | 17 | |
| α-helix | 79-92 | 14 | |
| α-helix | 97-114 | 18 | |
| α-helix | 118-134 | 17 | |
| α-helix | 139-154 | 16 | |
| α-helix | 158-174 | 17 | |
| α-helix | 178-193 | 16 | |
| α-helix | 198-201 | 4 | |
| α-helix | 202-216 | 15 | |
| α-helix | 218-231 | 14 | |
| α-helix | 233-236 | 4 | |
| α-helix | 239-251 | 13 | |
| α-helix | 256-269 | 14 | |
| α-helix | 274-286 | 13 | |
Chain F: 17 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-24 | 23 | |
| α-helix | 35-54 | 20 | |
| α-helix | 58-74 | 17 | |
| α-helix | 79-92 | 14 | |
| α-helix | 97-114 | 18 | |
| α-helix | 118-134 | 17 | |
| α-helix | 139-154 | 16 | |
| α-helix | 158-174 | 17 | |
| α-helix | 178-194 | 17 | |
| α-helix | 198-200 | 3 | |
| α-helix | 202-216 | 15 | |
| α-helix | 218-231 | 14 | |
| α-helix | 233-236 | 4 | |
| α-helix | 238-252 | 15 | |
| α-helix | 256-269 | 14 | |
| α-helix | 271-273 | 3 | |
| α-helix | 274-286 | 13 | |
Chain G: 16 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-22 | 21 | |
| α-helix | 35-55 | 21 | |
| α-helix | 60-74 | 15 | |
| α-helix | 79-95 | 17 | |
| α-helix | 97-113 | 17 | |
| α-helix | 117-133 | 17 | |
| α-helix | 138-153 | 16 | |
| α-helix | 163-174 | 12 | |
| α-helix | 178-194 | 17 | |
| α-helix | 199-216 | 18 | |
| α-helix | 218-231 | 14 | |
| α-helix | 234-237 | 4 | |
| α-helix | 239-250 | 12 | |
| α-helix | 256-269 | 14 | |
| α-helix | 274-283 | 10 | |
| α-helix | 284-288 | 5 | |
Chain H: 17 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-25 | 23 | |
| α-helix | 36-54 | 19 | |
| α-helix | 58-74 | 17 | |
| α-helix | 79-92 | 14 | |
| α-helix | 97-114 | 18 | |
| α-helix | 118-130 | 13 | |
| α-helix | 131-135 | 5 | |
| α-helix | 138-154 | 17 | |
| α-helix | 158-174 | 17 | |
| α-helix | 178-193 | 16 | |
| α-helix | 198-201 | 4 | |
| α-helix | 202-216 | 15 | |
| α-helix | 218-231 | 14 | |
| α-helix | 233-236 | 4 | |
| α-helix | 239-253 | 15 | |
| α-helix | 256-269 | 14 | |
| α-helix | 274-290 | 17 | |
Chain J: 7 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-10 | 7 | 1 |
| α-helix | 11-12 | 2 | |
| α-helix | 14-18 | 5 | |
| β-strand | 22-25 | 4 | 1 |
| β-strand | 34-40 | 7 | 1 |
| β-strand | 43-52 | 10 | 1 |
| α-helix | 55-56 | 2 | |
| β-strand | 59-62 | 4 | 1 |
| α-helix | 64-70 | 7 | |
| β-strand | 77-82 | 6 | 1 |
| β-strand | 92-101 | 10 | 2 |
| α-helix | 104-106 | 3 | |
| β-strand | 111-113 | 3 | 3 |
| α-helix | 114-125 | 12 | |
| β-strand | 129-131 | 3 | 4 |
| β-strand | 135-140 | 6 | 2 |
| β-strand | 143-153 | 11 | 2 |
| β-strand | 174-176 | 3 | 4 |
| β-strand | 177-187 | 11 | 2 |
| α-helix | 188 | 1 | |
| β-strand | 194-196 | 3 | 3 |
| β-strand | 200 | 1 | 2 |
1 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Synaptosomal-associated protein 25 | A, C | protein | 84 | Rattus norvegicus | P60881 (AlphaFold model) |
| Syntaxin-1A | B, D | protein | 78 | Rattus norvegicus | P32851 (AlphaFold model) |
| Alpha-soluble NSF attachment protein | E, F, G, H | protein | 296 | Rattus norvegicus | P54921 (AlphaFold model) |
| Vesicle-fusing ATPase | J, K | protein | 747 | Cricetulus griseus | P18708 (AlphaFold model) |
Sequence of entity 1 (A, C), FASTA
>9PFG_1 Synaptosomal-associated protein 25 (chains A, C)
SMAEDADMRNELEEMQRRADQLADESLESTRRMLQLVEESKDAGIRTLVMLDEQGEQLER
IEEGMDQINKDMKEAEKNLTDLGK
Sequence of entity 2 (B, D), FASTA
>9PFG_2 Syntaxin-1A (chains B, D)
MALSEIETRHSEIIKLENSIRELHDMFMDMAMLVESQGEMIDRIEYNVEHAVDYVERAVS
DTKKAVKYQSKARRKKIM
Sequence of entity 3 (E, F, G, H), FASTA
>9PFG_3 Alpha-soluble NSF attachment protein (chains E, F, G, H)
GMDTSGKQAEAMALLAEAERKVKNSQSFFSGLFGGSSKIEEACEIYARAANMFKMAKNWS
AAGNAFCQAAQLHLQLQSKHDAATCFVDAGNAFKKADPQEAINCLMRAIEIYTDMGRFTI
AAKHHISIAEIYETELVDVEKAIAHYEQSADYYKGEESNSSANKCLLKVAGYAAQLEQYQ
KAIDIYEQVGTSAMDSPLLKYSAKDYFFKAALCHFCIDMLNAKLAVQKYEELFPAFSDSR
ECKLMKKLLEAHEEQNVDSYTESVKEYDSISRLDQWLTTMLLRIKKTIQGDEEDLR
Sequence of entity 4 (J, K), FASTA
>9PFG_4 Vesicle-fusing ATPase (chains J, K)
GAHMAGRSMQAARCPTDELSLSNCAVVSEKDYQSGQHVIVRTSPNHKYIFTLRTHPSVVP
GSVAFSLPQRKWAGLSIGQEIEVALYSFDKAKQCIGTMTIEIDFLQKKNIDSNPYDTDKM
AAEFIQQFNNQAFSVGQQLVFSFNDKLFGLLVKDIEAMDPSILKGEPASGKRQKIEVGLV
VGNSQVAFEKAENSSLNLIGKAKTKENRQSIINPDWNFEKMGIGGLDKEFSDIFRRAFAS
RVFPPEIVEQMGCKHVKGILLYGPPGCGKTLLARQIGKMLNAREPKVVNGPEILNKYVGE
SEANIRKLFADAEEEQRRLGANSGLHIIIFDEIDAICKQRGSMAGSTGVHDTVVNQLLSK
IDGVEQLNNILVIGMTNRPDLIDEALLRPGRLEVKMEIGLPDEKGRLQILHIHTARMRGH
QLLSADVDIKELAVETKNFSGAELEGLVRAAQSTAMNRHIKASTKVEVDMEKAESLQVTR
GDFLASLENDIKPAFGTNQEDYASYIMNGIIKWGDPVTRVLDDGELLVQQTKNSDRTPLV
SVLLEGPPHSGKTALAAKIAEESNFPFIKICSPDKMIGFSETAKCQAMKKIFDDAYKSQL
SCVVVDDIERLLDYVPIGPRFSNLVLQALLVLLKKAPPQGRKLLIIGTTSRKDVLQEMEM
LNAFSTTIHVPNIATGEQLLEALELLGNFKDKERTTIAQQVKGKKVWIGIKKLLMLIEMS
LQMDPEYRVRKFLALLREEGASPLDFD
Primary citation
Structural remodeling of target-SNARE protein complexes by NSF enables synaptic transmission. White, K.I., Khan, Y.A., Qiu, K. et al. Nat Commun (2025) 16:8371-8371. DOI 10.1038/s41467-025-62764-0 · PubMed
Other PDB entries of the same protein (UniProt P60881 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 1N7S 1.45 Å, High Resolution Structure of a Truncated Neuronal SNARE Complex
- 5W5C 1.85 Å, Crystal structure of the primed SNARE-Complexin-Synaptotagmin-1 C2AB complex
- 1JTH 2.0 Å, Crystal structure and biophysical properties of a complex between the N-terminal region…
- 1URQ 2.0 Å, Crystal structure of neuronal Q-SNAREs in complex with R-SNARE motif of Tomosyn
- 6WVW 2.11 Å, Crystal structure of the R59P-SNAP25 containing SNARE complex
- 1SFC 2.4 Å, Neuronal synaptic fusion complex
- 5W5D 2.5 Å, Crystal structure of the primed SNARE-Complexin-Synaptotagmin-1 C2B complex
- 5LOW 2.8 Å, Structure of the Ca2+-bound Rabphilin 3A C2B domain SNAP25 complex (P21 space group)
- 9OJR 2.95 Å, 21bin20S complex (NSF-alphaSNAP-2:1 syntaxin-1a:SNAP-25), non-hydrolyzing, class 3
- 9OJU 2.97 Å, 21bin20S complex (NSF-alphaSNAP-2:1 syntaxin-1a:SNAP-25), non-hydrolyzing, class 4
- 9PFF 3.09 Å, Min22bin20S complex (NSF-alphaSNAP-2:2 syntaxin-1a H3:SNAP-25 SN1), non-hydrolyzing,…
- 5LOB 3.3 Å, Structure of the Ca2+-bound Rabphilin3A C2B- SNAP25 complex (C2 space group)
Browse structure collections
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