6IP1: Vesicle-associated membrane protein 2
alpha-SNAP-SNARE subcomplex in the whole 20S complex. Determined by electron microscopy at 3.9 Å resolution. Released 24 Apr 2019.
- Method
- Electron microscopy
- Resolution
- 3.9 Å
- Organisms
- Rattus norvegicus, Bos taurus
- Chains
- 8
- Atoms
- 11,245
- Mol. weight
- 199.94 kDa
- Released
- 24 Apr 2019
Explore 6IP1 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
6IP1 contains 76 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.
Chain A: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 29-82 | 54 | |
Chain B: 2 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 193-227 | 35 | |
| α-helix | 231-251 | 21 | |
Chain C: 4 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 18-36 | 19 | |
| α-helix | 38-66 | 29 | |
| α-helix | 69-76 | 8 | |
| α-helix | 77-79 | 3 | |
Chain D: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 143-200 | 58 | |
Chains E, F and H: 17 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 6-19 | 14 | |
| α-helix | 24-26 | 3 | |
| α-helix | 40-54 | 15 | |
| α-helix | 58-74 | 17 | |
| α-helix | 78-89 | 12 | |
| α-helix | 92-94 | 3 | |
| α-helix | 97-112 | 16 | |
| α-helix | 118-133 | 16 | |
| α-helix | 138-154 | 17 | |
| α-helix | 158-174 | 17 | |
| α-helix | 178-193 | 16 | |
| α-helix | 202-211 | 10 | |
| α-helix | 222-231 | 10 | |
| α-helix | 234-237 | 4 | |
| α-helix | 240-251 | 12 | |
| α-helix | 258-267 | 10 | |
| α-helix | 274-294 | 21 | |
Chain G: 17 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 6-19 | 14 | |
| α-helix | 24-26 | 3 | |
| α-helix | 40-54 | 15 | |
| α-helix | 58-74 | 17 | |
| α-helix | 82-89 | 8 | |
| α-helix | 92-94 | 3 | |
| α-helix | 97-112 | 16 | |
| α-helix | 118-133 | 16 | |
| α-helix | 138-154 | 17 | |
| α-helix | 158-174 | 17 | |
| α-helix | 178-193 | 16 | |
| α-helix | 203-211 | 9 | |
| α-helix | 222-231 | 10 | |
| α-helix | 234-237 | 4 | |
| α-helix | 240-251 | 12 | |
| α-helix | 258-267 | 10 | |
| α-helix | 274-294 | 21 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Vesicle-associated membrane protein 2 | A | protein | 97 | Rattus norvegicus | P63045 (AlphaFold model) |
| Syntaxin-1A | B | protein | 254 | Rattus norvegicus | P32851 (AlphaFold model) |
| Synaptosomal-associated protein 25 | C | protein | 102 | Rattus norvegicus | P60881 (AlphaFold model) |
| Synaptosomal-associated protein 25 | D | protein | 83 | Rattus norvegicus | P60881 (AlphaFold model) |
| Alpha-soluble NSF attachment protein | E, F, G, H | protein | 309 | Bos taurus | P81125 (AlphaFold model) |
Sequence of entity 1 (A), FASTA
>6IP1_1 Vesicle-associated membrane protein 2 (chains A)
GSHMSATAATVPPAAPAGEGGPPAPPPNLTSNRRLQQTQAQVDEVVDIMRVNVDKVLERD
QKLSELDDRADALQAGASQFETSAAKLKRKYWWKNLK
Sequence of entity 2 (B), FASTA
>6IP1_2 Syntaxin-1A (chains B)
GSKDRTQELRTAKDSDDDDDVTVTVDRDRFMDEFFEQVEEIRGFIDKIAENVEEVKRKHS
AILASPNPDEKTKEELEELMSDIKKTANKVRSKLKSIEQSIEQEEGLNRSSADLRIRKTQ
HSTLSRKFVEVMSEYNATQSDYRERCKGRIQRQLEITGRTTTSEELEDMLESGNPAIFAS
GIIMDSSISKQALSEIETRHSEIIKLENSIRELHDMFMDMAMLVESQGEMIDRIEYNVEH
AVDYVERAVSDTKK
Sequence of entity 3 (C), FASTA
>6IP1_3 Synaptosomal-associated protein 25 (chains C)
GSMAEDADMRNELEEMQRRADQLADESLESTRRMLQLVEESKDAGIRTLVMLDEQGEQLE
RIEEGMDQINKDMKEAEKNLTDLGKFCGLCVCPCNKLKSSDA
Sequence of entity 4 (D), FASTA
>6IP1_4 Synaptosomal-associated protein 25 (chains D)
GSQMAISGGFIRRVTNDARENEMDENLEQVSGIIGNLRHMALDMGNEIDTQNRQIDRIME
KADSNKTRIDEANQRATKMLGSG
Sequence of entity 5 (E, F, G, H), FASTA
>6IP1_5 Alpha-soluble NSF attachment protein (chains E, F, G, H)
GSMRGSHHHHHHGSMDNSGKEAEAMALLAEAERKVKNSQSFFSGLFGGSSKIEEACEIYA
RAANMFKMAKNWSAAGSAFCQAAQLHLQLQSKHDAATCFVDAGNAFKKADPQEAINCLMR
AIEIYTDMGRFTIAAKHHISIAEIYETELVDIEKAIAHYEQSADYYKGEESNSSANKCLL
KVAGYAAQLEQYQKAIDIYEQVGTNAMDSPLLKYSAKDYFFKAALCHFCIDMLNAKLAVQ
KYEELFPAFSDSRECKLMKKLLEAHEEQNVDSYTEAVKEYDSISRLDQWLTTMLLRIKKT
IQGDEEDLR
Primary citation
Mechanistic insights into the SNARE complex disassembly. Huang, X., Sun, S., Wang, X. et al. Sci Adv (2019) 5:eaau8164-eaau8164. DOI 10.1126/sciadv.aau8164 · PubMed
Other PDB entries of the same protein (UniProt P63045 (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
- 6WVW 2.11 Å, Crystal structure of the R59P-SNAP25 containing SNARE complex
- 1KIL 2.3 Å, Three-dimensional structure of the complexin/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
- 6A30 2.79 Å, Crystal Structure of Munc13-1 MUN Domain and Synaptobrevin-2 Juxtamembrane Linker Region
- 3HD7 3.4 Å, Helical extension of the neuronal snare complex into the membrane, spacegroup C 1 2 1
- 5CCG 3.5 Å, Structure of the Ca2+-bound synaptotagmin-1 SNARE complex (long unit cell form)
- 7UDB 3.5 Å, Cryo-EM structure of a synaptobrevin-Munc18-1-syntaxin-1 complex class 2
- 5CCH 3.6 Å, Structure of the Ca2+-bound synaptotagmin-1 SNARE complex (short unit cell form)
- 5CCI 4.1 Å, Structure of the Mg2+-bound synaptotagmin-1 SNARE complex (short unit cell form)
Browse structure collections
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