5NIY: Signal recognition particle-docking protein FtsY

Signal recognition particle-docking protein FtsY. Determined by X-ray diffraction at 1.7 Å resolution. Released 10 Oct 2018.

Method: X-ray diffraction
Resolution: 1.7 Å
Organism: Escherichia coli
Chains: 1
Atoms: 2,650
Mol. weight: 34.53 kDa
Ligands: GNP
Released: 10 Oct 2018

Explore 5NIY in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5NIY contains 17 α-helices and 11 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.

Chain A: 17 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	198-202	5
α-helix	206-208	3
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	283	1	2
β-strand	294-299	6	2
α-helix	306-319	14
β-strand	324-327	4	2
α-helix	334-346	13
β-strand	351-352	2	2
α-helix	360-373	14
β-strand	378-381	4	2
α-helix	390-404	15
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

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Signal recognition particle-docking protein FtsY	A	protein	309	Escherichia coli	P10121 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>5NIY_1 Signal recognition particle-docking protein FtsY (chains A)
MFARLKRSLLKTKENLGSGFISLFRGKKIDDDLFEELEEQLLIADVGVETTRKIITNLTE
GASRKQLRDAEALYGLLKEEMGEILAKVDEPLNVEGKAPFVILMVGVNGVGKTTTIGKLA
RQFEQQGKSVMLAAGDTFRAAAVEQLQVWGQRNNIPVIAQHTGADSASVIFDAIQAAKAR
NIDVLIADTAGRLQNKSHLMEELKKIVRVMKKLDVEAPHEVMLTIDASTGQNAVSQAKLF
HEAVGLTGITLTKLDGTAKGGVIFSVADQFGIPIRYIGVGERIEDLRPFKADDFIEALFA
REDHHHHHH

Ligands and cofactors

ID	Name	Formula	Copies
GNP	Phosphoaminophosphonic acid-guanylate ester	C10 H17 N6 O13 P3	1

Primary citation

The Escherichia coli SRP Receptor Forms a Homodimer at the Membrane. Kempf, G., Stjepanovic, G., Sloan, J. et al. Structure (2018) 26:1440-1450.e5. DOI 10.1016/j.str.2018.07.008 · PubMed

Other PDB entries of the same protein (UniProt P10121 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6N9B 1.22 Å, FtsY-NG ultra high-resolution
6N5J 1.37 Å, FtsY-NG high-resolution
6CQP 1.45 Å, High resolution crystal structure of FtsY-NG domain of E. coli
6N5I 1.5 Å, FtsY-NG high-resolution
6NC1 1.6 Å, FtsY-NG high-resolution
2YHS 1.6 Å, Structure of the E. coli SRP receptor FtsY
6NC4 1.6 Å, FtsY-NG high-resolution
6CS8 1.75 Å, High resolution crystal structure of FtsY-NG domain of E. coli
6CVD 1.78 Å, High resolution crystal structure of FtsY-NG domain of E. coli bound to fragment 1
6DLX 1.85 Å, FtsY-NG domain bound to fragment 3.
6N6N 1.88 Å, FtsY-NG high-resolution
2QY9 1.9 Å, Structure of the NG+1 construct of the E. coli SRP receptor FtsY

Browse structure collections

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