9OM6: Syntaxin-1A
22bin20S complex (NSF-alphaSNAP-2:2 syntaxin-1a:SNAP-25), 4:2:2 alphaSNAP-syntaxin-1a-SNAP-25 subcomplex local refinement, hydrolyzing, class 23. Determined by electron microscopy at 4.14 Å resolution. Released 6 Aug 2025.
- Method
- Electron microscopy
- Resolution
- 4.14 Å
- Organism
- Rattus norvegicus
- Chains
- 8
- Atoms
- 11,330
- Mol. weight
- 245.33 kDa
- Released
- 6 Aug 2025
Explore 9OM6 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
9OM6 contains 68 α-helices and 0 β-strands across 8 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.
Chains A and B: 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 | 18-85 | 68 | |
Chain D: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 18-82 | 65 | |
Chain E: 17 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 1-28 | 28 | |
| α-helix | 34-54 | 21 | |
| α-helix | 58-72 | 15 | |
| α-helix | 73-75 | 3 | |
| α-helix | 79-93 | 15 | |
| α-helix | 98-114 | 17 | |
| α-helix | 117-134 | 18 | |
| α-helix | 139-154 | 16 | |
| α-helix | 158-175 | 18 | |
| α-helix | 178-193 | 16 | |
| α-helix | 198-201 | 4 | |
| α-helix | 202-216 | 15 | |
| α-helix | 219-231 | 13 | |
| α-helix | 233-236 | 4 | |
| α-helix | 240-253 | 14 | |
| α-helix | 256-267 | 12 | |
| α-helix | 274-285 | 12 | |
Chain F: 16 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 1-31 | 31 | |
| α-helix | 36-54 | 19 | |
| α-helix | 58-74 | 17 | |
| α-helix | 79-93 | 15 | |
| α-helix | 98-114 | 17 | |
| α-helix | 118-134 | 17 | |
| α-helix | 138-154 | 17 | |
| α-helix | 158-174 | 17 | |
| α-helix | 179-191 | 13 | |
| α-helix | 198-201 | 4 | |
| α-helix | 202-213 | 12 | |
| α-helix | 219-231 | 13 | |
| α-helix | 233-237 | 5 | |
| α-helix | 239-252 | 14 | |
| α-helix | 256-269 | 14 | |
| α-helix | 274-284 | 11 | |
Chain G: 15 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 1-30 | 30 | |
| α-helix | 36-54 | 19 | |
| α-helix | 59-73 | 15 | |
| α-helix | 79-92 | 14 | |
| α-helix | 97-114 | 18 | |
| α-helix | 118-133 | 16 | |
| α-helix | 139-154 | 16 | |
| α-helix | 158-174 | 17 | |
| α-helix | 179-189 | 11 | |
| α-helix | 203-216 | 14 | |
| α-helix | 218-231 | 14 | |
| α-helix | 233-237 | 5 | |
| α-helix | 239-253 | 15 | |
| α-helix | 256-269 | 14 | |
| α-helix | 276-285 | 10 | |
Chain H: 16 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 1-25 | 25 | |
| α-helix | 27-29 | 3 | |
| α-helix | 35-55 | 21 | |
| α-helix | 58-72 | 15 | |
| α-helix | 78-93 | 16 | |
| α-helix | 98-114 | 17 | |
| α-helix | 117-134 | 18 | |
| α-helix | 139-154 | 16 | |
| α-helix | 158-174 | 17 | |
| α-helix | 178-189 | 12 | |
| α-helix | 202-216 | 15 | |
| α-helix | 218-231 | 14 | |
| α-helix | 233-235 | 3 | |
| α-helix | 239-251 | 13 | |
| α-helix | 256-267 | 12 | |
| α-helix | 274-284 | 11 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Syntaxin-1A | A, B | protein | 267 | Rattus norvegicus | P32851 (AlphaFold model) |
| Synaptosomal-associated protein 25 | C, D | protein | 222 | Rattus norvegicus | P60881 (AlphaFold model) |
| Alpha-soluble NSF attachment protein | E, F, G, H | protein | 296 | Rattus norvegicus | P54921 (AlphaFold model) |
Sequence of entity 1 (A, B), FASTA
>9OM6_1 Syntaxin-1A (chains A, B)
MKDRTQELRTAKDSDDDDDVTVTVDRDRFMDEFFEQVEEIRGFIDKIAENVEEVKRKHSA
ILASPNPDEKTKEELEELMSDIKKTANKVRSKLKSIEQSIEQEEGLNRSSADLRIRKTQH
STLSRKFVEVMSEYNATQSDYRERCKGRIQRQLEITGRTTTSEELEDMLESGNPAIFASG
IIMDSSISKQALSEIETRHSEIIKLENSIRELHDMFMDMAMLVESQGEMIDRIEYNVEHA
VDYVERAVSDTKKAVKYQSKARRKKIM
Sequence of entity 2 (C, D), FASTA
>9OM6_2 Synaptosomal-associated protein 25 (chains C, D)
MGSSHHHHHHSQDPNSMAEDADMRNELEEMQRRADQLADESLESTRRMLQLVEESKDAGI
RTLVMLDEQGEQLERIEEGMDQINKDMKEAEKNLTDLGKFAGLAVAPANKLKSSDAYKKA
WGNNQDGVVASQPARVVDEREQMAISGGFIRRVTNDARENEMDENLEQVSGIIGNLRHMA
LDMGNEIDTQNRQIDRIMEKADSNKTRIDEANQRATKMLGSG
Sequence of entity 3 (E, F, G, H), FASTA
>9OM6_3 Alpha-soluble NSF attachment protein (chains E, F, G, H)
GMDTSGKQAEAMALLAEAERKVKNSQSFFSGLFGGSSKIEEACEIYARAANMFKMAKNWS
AAGNAFCQAAQLHLQLQSKHDAATCFVDAGNAFKKADPQEAINCLMRAIEIYTDMGRFTI
AAKHHISIAEIYETELVDVEKAIAHYEQSADYYKGEESNSSANKCLLKVAGYAAQLEQYQ
KAIDIYEQVGTSAMDSPLLKYSAKDYFFKAALCHFCIDMLNAKLAVQKYEELFPAFSDSR
ECKLMKKLLEAHEEQNVDSYTESVKEYDSISRLDQWLTTMLLRIKKTIQGDEEDLR
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 P32851 (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
- 1EZ3 1.9 Å, Crystal structure of the neuronal T-snare syntaxin-1A
- 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
- 3RK2 2.2 Å, Truncated SNARE complex
- 1KIL 2.3 Å, Three-dimensional structure of the complexin/SNARE complex
- 1HVV 2.4 Å, Self-association of the H3 region of syntaxin 1A: implications for snare complex assembly
- 1SFC 2.4 Å, Neuronal synaptic fusion complex
- 5W5D 2.5 Å, Crystal structure of the primed SNARE-Complexin-Synaptotagmin-1 C2B complex
- 4JEH 2.5 Å, Crystal Structure of Munc18a and Syntaxin1 lacking N-peptide complex
Browse structure collections
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