Cesium sites in the crystal structure of acid-sensing ion channel in complex with snake toxin. Determined by X-ray diffraction at 2.65 Å resolution. Released 19 Feb 2014.
Explore 4NTY in 3D Show helices and sheets RCSB PDB PDBe
4NTY contains 36 α-helices and 26 β-strands across 3 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 | 48-69 | 22 | |
| β-strand | 74-81 | 8 | 1 |
| β-strand | 86-87 | 2 | 2 |
| β-strand | 90-95 | 6 | 3 |
| α-helix | 101-103 | 3 | |
| α-helix | 106-112 | 7 | |
| α-helix | 133-142 | 10 | |
| α-helix | 150-152 | 3 | |
| α-helix | 155-162 | 8 | |
| α-helix | 166-169 | 4 | |
| β-strand | 170-175 | 6 | 1 |
| β-strand | 178-179 | 2 | 1 |
| α-helix | 182-184 | 3 | |
| β-strand | 185-190 | 6 | 3 |
| β-strand | 193-198 | 6 | 3 |
| α-helix | 205-208 | 4 | |
| β-strand | 209-210 | 2 | 2 |
| α-helix | 215-217 | 3 | |
| β-strand | 219-224 | 6 | 1 |
| α-helix | 227-229 | 3 | |
| α-helix | 231-232 | 2 | |
| β-strand | 246-251 | 6 | 3 |
| α-helix | 259-262 | 4 | |
| β-strand | 264-266 | 3 | 3 |
| β-strand | 270-282 | 13 | 1 |
| α-helix | 284-285 | 2 | |
| β-strand | 291-292 | 2 | 4 |
| α-helix | 306-322 | 17 | |
| β-strand | 325 | 1 | 5 |
| α-helix | 334 | 1 | |
| β-strand | 335 | 1 | 5 |
| α-helix | 336-337 | 2 | |
| α-helix | 338-340 | 3 | |
| α-helix | 341-345 | 5 | |
| α-helix | 346-354 | 9 | |
| α-helix | 362-363 | 2 | |
| β-strand | 364-365 | 2 | 4 |
| β-strand | 367-379 | 13 | 1 |
| α-helix | 386-393 | 8 | |
| α-helix | 397-403 | 7 | |
| β-strand | 404-411 | 8 | 1 |
| β-strand | 416-423 | 8 | 1 |
| α-helix | 428-441 | 14 | |
| α-helix | 446-452 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-8 | 3 | |
| α-helix | 10-11 | 2 | |
| β-strand | 21-27 | 7 | 6 |
| β-strand | 32-38 | 7 | 6 |
| β-strand | 48 | 1 | 6 |
| α-helix | 51-57 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2-12 | 11 | |
| α-helix | 18-21 | 4 | |
| β-strand | 23 | 1 | 7 |
| α-helix | 39-52 | 14 | |
| α-helix | 53-57 | 5 | |
| β-strand | 69 | 1 | 8 |
| α-helix | 74-76 | 3 | |
| β-strand | 78 | 1 | 8 |
| α-helix | 85-103 | 19 | |
| α-helix | 108-110 | 3 | |
| β-strand | 111 | 1 | 7 |
| α-helix | 115-117 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Acid-sensing ion channel 1 | A | protein | 450 | Gallus gallus | Q1XA76 (AlphaFold model) |
| Neurotoxin MitTx-alpha | B | protein | 60 | Micrurus tener tener | G9I929 (AlphaFold model) |
| Basic phospholipase A2 homolog Tx-beta | C | protein | 119 | Micrurus tener tener | G9I930 (AlphaFold model) |
>4NTY_1 Acid-sensing ion channel 1 (chains A) GQPVSIQAFASSSTLHGISHIFSYERLSLKRVVWALCFMGSLALLALVCTNRIQYYFLYP HVTKLDEVAATRLTFPAVTFCNLNEFRFSRVTKNDLYHAGELLALLNNRYEIPDTQTADE KQLEILQDKANFRNFKPKPFNMLEFYDRAGHDIREMLLSCFFRGEQCSPEDFKVVFTRYG KCYTFNAGQDGKPRLITMKGGTGNGLEIMLDIQQDEYLPVWGETDETSFEAGIKVQIHSQ DEPPLIDQLGFGVAPGFQTFVSCQEQRLIYLPPPWGDCKATTGDSEFYDTYSITACRIDC ETRYLVENCNCRMVHMPGDAPYCTPEQYKECADPALDFLVEKDNEYCVCEMPCNVTRYGK ELSMVKIPSKASAKYLAKKYNKSEQYIGENILVLDIFFEALNYETIEQKKAYEVAGLLGD IGGQMGLFIGASILTVLELFDYAYEVIKHR
>4NTY_2 Neurotoxin MitTx-alpha (chains B) QIRPAFCYEDPPFFQKCGAFVDSYYFNRSRITCVHFFYGQCDVNQNHFTTMSECNRVCHG
>4NTY_3 Basic phospholipase A2 homolog Tx-beta (chains C) NLNQFRLMIKCTNDRVWADFVDYGCYCVARDSNTPVDDLDRCCQAQKQCYDEAVKVHGCK PLVMFYSFECRYLASDLDCSGNNTKCRNFVCNCDRTATLCILTATYNRNNHKIDPSRCQ
| ID | Name | Formula | Copies |
|---|---|---|---|
| PE4 | 2-{2-[2-(2-{2-[2-(2-ethoxy-ethoxy)-ethoxy]-ethoxy}-ethoxy)-ethoxy]-ethoxy}-etha… | C16 H34 O8 | 1 |
| CS | Cesium ion | Cs | 15 |
Water and common crystallization additives (CL) are not listed.
X-ray structure of Acid-sensing ion channel 1-snake toxin complex reveals open state of a na(+)-selective channel. Baconguis, I., Bohlen, C.J., Goehring, A. et al. Cell (2014) 156:717-729. DOI 10.1016/j.cell.2014.01.011 · PubMed
Other PDB entries of the same protein (UniProt Q1XA76 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 4NTY directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.