FtsY-NG high-resolution. Determined by X-ray diffraction at 1.88 Å resolution. Released 9 Oct 2019.
Explore 6N6N in 3D Show helices and sheets RCSB PDB PDBe
6N6N contains 36 α-helices and 20 β-strands across 2 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 | 197-202 | 6 | |
| α-helix | 204-207 | 4 | |
| α-helix | 213-218 | 6 | |
| β-strand | 222 | 1 | 1 |
| α-helix | 225-237 | 13 | |
| α-helix | 242-258 | 17 | |
| β-strand | 263 | 1 | 1 |
| α-helix | 264-266 | 3 | |
| α-helix | 267-280 | 14 | |
| β-strand | 294-299 | 6 | 2 |
| α-helix | 306-319 | 14 | |
| β-strand | 324-327 | 4 | 2 |
| α-helix | 334-347 | 14 | |
| β-strand | 351-352 | 2 | 2 |
| α-helix | 360-373 | 14 | |
| β-strand | 378-381 | 4 | 2 |
| α-helix | 390-407 | 18 | |
| β-strand | 414-420 | 7 | 2 |
| α-helix | 421-423 | 3 | |
| α-helix | 425-437 | 13 | |
| β-strand | 442-446 | 5 | 2 |
| α-helix | 456-464 | 9 | |
| β-strand | 468-472 | 5 | 2 |
| α-helix | 477-479 | 3 | |
| β-strand | 480-482 | 3 | 2 |
| α-helix | 483 | 1 | |
| α-helix | 485-493 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 196-202 | 7 | |
| α-helix | 204-207 | 4 | |
| α-helix | 211-214 | 4 | |
| α-helix | 215-218 | 4 | |
| β-strand | 222 | 1 | 3 |
| α-helix | 225-237 | 13 | |
| α-helix | 242-259 | 18 | |
| β-strand | 263 | 1 | 3 |
| α-helix | 264-266 | 3 | |
| α-helix | 267-280 | 14 | |
| β-strand | 294-299 | 6 | 4 |
| α-helix | 306-319 | 14 | |
| β-strand | 324-327 | 4 | 4 |
| α-helix | 334-346 | 13 | |
| β-strand | 351-352 | 2 | 4 |
| α-helix | 360-373 | 14 | |
| β-strand | 378-381 | 4 | 4 |
| α-helix | 390-407 | 18 | |
| β-strand | 414-420 | 7 | 4 |
| α-helix | 421-423 | 3 | |
| α-helix | 425-437 | 13 | |
| β-strand | 442-446 | 5 | 4 |
| α-helix | 448-450 | 3 | |
| α-helix | 456-464 | 9 | |
| β-strand | 468-472 | 5 | 4 |
| α-helix | 477-479 | 3 | |
| β-strand | 480-482 | 3 | 4 |
| α-helix | 483 | 1 | |
| α-helix | 485-493 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Signal recognition particle receptor FtsY | A, B | protein | 303 | Escherichia coli (strain K12) | P10121 (AlphaFold model) |
>6N6N_1 Signal recognition particle receptor FtsY (chains A, B) GFARLKRSLLKTKENLGSGFISLFRGKKIDDDLFEELEEQLLIADVGVETTRKIITNLTE GASRKQLRDAEALYGLLKEEMGEILAKVDEPLNVEGKAPFVILMVGVNGVGKTTTIGKLA RQFEQQGKSVMLAAGDTFRAAAVEQLQVWGQRNNIPVIAQHTGADSASVIFDAIQAAKAR NIDVLIADTAGRLQNKSHLMEELKKIVRVMKKLDVEAPHEVMLTIDASTGQNAVSQAKLF HEAVGLTGITLTKLDGTAKGGVIFSVADQFGIPIRYIGVGERIEDLRPFKADDFIEALFA RED
| ID | Name | Formula | Copies |
|---|---|---|---|
| GCP | Phosphomethylphosphonic acid guanylate ester | C11 H18 N5 O13 P3 | 2 |
| MG | Magnesium ion | Mg | 5 |
Water and common crystallization additives (ACT, GOL) are not listed.
Structural insights into the G-loop dynamics of E. coli FtsY NG domain. Faoro, C., Ataide, S.F. J Struct Biol (2019) 208:107387-107387. DOI 10.1016/j.jsb.2019.09.004 · PubMed
Other PDB entries of the same protein (UniProt P10121 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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