The crystal structure of cpFtsY from Arabidopsis thaliana. Determined by X-ray diffraction at 1.75 Å resolution. Released 25 Dec 2007.
Explore 3B9Q in 3D Show helices and sheets RCSB PDB PDBe
3B9Q contains 17 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 | 66-70 | 5 | |
| α-helix | 72-78 | 7 | |
| α-helix | 80-85 | 6 | |
| α-helix | 90-92 | 3 | |
| α-helix | 93-106 | 14 | |
| α-helix | 111-126 | 16 | |
| α-helix | 133-148 | 16 | |
| β-strand | 165-170 | 6 | 1 |
| α-helix | 177-190 | 14 | |
| β-strand | 195-198 | 4 | 1 |
| α-helix | 205-218 | 14 | |
| β-strand | 221-223 | 3 | 1 |
| α-helix | 232-245 | 14 | |
| β-strand | 250-253 | 4 | 1 |
| α-helix | 263-277 | 15 | |
| β-strand | 286-292 | 7 | 1 |
| α-helix | 293-299 | 7 | |
| α-helix | 300-309 | 10 | |
| β-strand | 314-318 | 5 | 1 |
| α-helix | 327-336 | 10 | |
| α-helix | 338-339 | 2 | |
| β-strand | 340-344 | 5 | 1 |
| α-helix | 349-351 | 3 | |
| β-strand | 352-354 | 3 | 1 |
| α-helix | 357-365 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Chloroplast SRP receptor homolog, alpha subunit CPFTSY | A | protein | 302 | Arabidopsis thaliana | O80842 (AlphaFold model) |
>3B9Q_1 Chloroplast SRP receptor homolog, alpha subunit CPFTSY (chains A) EKVFSGFSKTRENLAVIDELLLFWNLAETDRVLDELEEALLVSDFGPKITVRIVERLRED IMSGKLKSGSEIKDALKESVLEMLAKKNSKTELQLGFRKPAVIMIVGVNGGGKTTSLGKL AHRLKNEGTKVLMAAGDTFRAAASDQLEIWAERTGCEIVVAEGDKAKAATVLSKAVKRGK EEGYDVVLCDTSGRLHTNYSLMEELIACKKAVGKIVSGAPNEILLVLDGNTGLNMLPQAR EFNEVVGITGLILTKLDGSARGGCVVSVVEELGIPVKFIGVGEAVEDLQPFDPEAFVNAI FS
| ID | Name | Formula | Copies |
|---|---|---|---|
| MLI | Malonate ion | C3 H2 O4 | 1 |
The structure of the chloroplast signal recognition particle (SRP) receptor reveals mechanistic details of SRP GTPase activation and a conserved membrane targeting site. Stengel, K.F., Holdermann, I., Wild, K. et al. FEBS Lett (2007) 581:5671-5676. DOI 10.1016/j.febslet.2007.11.024 · PubMed
Other PDB entries of the same protein (UniProt O80842 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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