3RL0: Truncated SNARE complex with complexin
Truncated SNARE complex with complexin (P1). Determined by X-ray diffraction at 3.8 Å resolution. Released 27 Jul 2011.
- Method
- X-ray diffraction
- Resolution
- 3.8 Å
- Organisms
- Homo sapiens, Rattus norvegicus
- Chains
- 40
- Atoms
- 17,672
- Mol. weight
- 288.38 kDa
- Released
- 27 Jul 2011
Explore 3RL0 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
3RL0 contains 41 α-helices and 0 β-strands across 40 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 | 11-78 | 68 | |
Chains A, E, Q and Y: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 27-59 | 33 | |
Chains b and H: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 140-198 | 59 | |
Chain B: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 192-248 | 57 | |
Chains c and I: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 28-59 | 32 | |
Chains C and G: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 9-77 | 69 | |
Chains d and J: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 191-247 | 57 | |
Chains D, f and T: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 140-199 | 60 | |
16 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 |
|---|
| Vesicle-associated membrane protein 2 | A, E, I, M, Q, U, Y, c | protein | 37 | Homo sapiens | P63027 (AlphaFold model) |
| Syntaxin-1A | B, F, J, N, R, V, Z, d | protein | 65 | Rattus norvegicus | P32851 (AlphaFold model) |
| Synaptosomal-associated protein 25 | C, G, K, O, S, W, a, e | protein | 81 | Homo sapiens | P60880 (AlphaFold model) |
| Synaptosomal-associated protein 25 | D, H, L, P, T, X, b, f | protein | 65 | Homo sapiens | P60880 (AlphaFold model) |
| Complexin-1 | g, h, i, j, k, l, m, n | protein | 63 | Homo sapiens | O14810 (AlphaFold model) |
Sequence of entity 1 (A, E, I, M, Q, U, Y, c), FASTA
>3RL0_1 Vesicle-associated membrane protein 2 (chains A, E, I, M, Q, U, Y, c)
GPLGSNRRLQQTQAQVDEVVDIMRVNVDKVLERDQKL
Sequence of entity 2 (B, F, J, N, R, V, Z, d), FASTA
>3RL0_2 Syntaxin-1A (chains B, F, J, N, R, V, Z, d)
GSALSEIETRHSEIIKLENSIRELHDMFMDMAMLVESQGEMIDRIEYNVEHAVDYVERAV
SDTKK
Sequence of entity 3 (C, G, K, O, S, W, a, e), FASTA
>3RL0_3 Synaptosomal-associated protein 25 (chains C, G, K, O, S, W, a, e)
GSHMMRNELEEMQRRADQLADESLESTRRMLQLVEESKDAGIRTLVMLDEQGEQLDRVEE
GMNHINQDMKEAEKNLKDLGW
Sequence of entity 4 (D, H, L, P, T, X, b, f), FASTA
>3RL0_4 Synaptosomal-associated protein 25 (chains D, H, L, P, T, X, b, f)
GSARENEMDENLEQVSGIIGNLRHMALDMGNEIDTQNRQIDRIMEKADSNKTRIDEANQR
ATKML
Sequence of entity 5 (g, h, i, j, k, l, m, n), FASTA
>3RL0_5 Complexin-1 (chains g, h, i, j, k, l, m, n)
GPLGSKLPDAAKKMEEAQEALRQAEEERKAKYAKMEAEREAVRQGIRDKYGIKKKEEREA
EAQ
Primary citation
Complexin cross-links prefusion SNAREs into a zigzag array. Kummel, D., Krishnakumar, S.S., Radoff, D.T. et al. Nat Struct Mol Biol (2011) 18:927-933. DOI 10.1038/nsmb.2101 · PubMed
Other PDB entries of the same protein (UniProt P63027 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 9CKX 1.98 Å, Crystal structure of Dsk2 Sti1 domain bound to a transmembrane domain
- 3FIE 2.1 Å, Crystal structure of Clostridium botulinum neurotoxin serotype F catalytic domain with…
- 3FII 2.17 Å, Crystal structure of Clostridium botulinum neurotoxin serotype F catalytic domain with…
- 3RK2 2.2 Å, Truncated SNARE complex
- 3RK3 3.5 Å, Truncated SNARE complex with complexin
- 7UDC 3.7 Å, cryo-EM structures of a synaptobrevin-Munc18-1-syntaxin-1 complex class1
Browse structure collections
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