T. aquaticus Ffh NG Domain at 1.1A Resolution. Determined by X-ray diffraction at 1.1 Å resolution. Released 16 Nov 2002.
Explore 1LS1 in 3D Show helices and sheets RCSB PDB PDBe
1LS1 contains 15 α-helices and 8 β-strands across 1 chain. 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 | 3-14 | 12 | |
| α-helix | 24-40 | 17 | |
| α-helix | 45-61 | 17 | |
| α-helix | 70-86 | 17 | |
| α-helix | 93-95 | 3 | |
| β-strand | 99-104 | 6 | 1 |
| α-helix | 111-124 | 14 | |
| β-strand | 129-133 | 5 | 1 |
| α-helix | 139-152 | 14 | |
| β-strand | 156-158 | 3 | 1 |
| α-helix | 159-160 | 2 | |
| α-helix | 165-179 | 15 | |
| β-strand | 183-187 | 5 | 1 |
| α-helix | 196-209 | 14 | |
| β-strand | 213-219 | 7 | 1 |
| α-helix | 220-222 | 3 | |
| α-helix | 224-236 | 13 | |
| β-strand | 241-245 | 5 | 1 |
| α-helix | 247-249 | 3 | |
| α-helix | 254-263 | 10 | |
| β-strand | 267-270 | 4 | 1 |
| β-strand | 280-281 | 2 | 1 |
| α-helix | 284-291 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Signal recognition particle protein | A | protein | 295 | Thermus aquaticus | O07347 (AlphaFold model) |
>1LS1_1 SIGNAL RECOGNITION PARTICLE PROTEIN (chains A) MFQQLSARLQEAIGRLRGRGRITEEDLKATLREIRRALMDADVNLEVARDFVERVREEAL GKQVLESLTPAEVILATVYEALKEALGGEARLPVLKDRNLWFLVGLQGSGKTTTAAKLAL YYKGKGRRPLLVAADTQRPAAREQLRLLGEKVGVPVLEVMDGESPESIRRRVEEKARLEA RDLILVDTAGRLQIDEPLMGELARLKEVLGPDEVLLVLDAMTGQEALSVARAFDEKVGVT GLVLTKLDGDARGGAALSARHVTGKPIYFAGVSEKPEGLEPFYPERLAGRILGMG
Structural Basis for Mobility in the 1.1 A Crystal Structure of the NG Domain of Thermus aquaticus Ffh. Ramirez, U.D., Minasov, G., Focia, P.J. et al. J Mol Biol (2002) 320:783-799. DOI 10.1016/S0022-2836(02)00476-X · PubMed
Other PDB entries of the same protein (UniProt O07347 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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