6CQP: FtsY-NG domain of E. coli

High resolution crystal structure of FtsY-NG domain of E. coli. Determined by X-ray diffraction at 1.45 Å resolution. Released 22 Aug 2018.

Method: X-ray diffraction
Resolution: 1.45 Å
Organism: Escherichia coli (strain K12)
Chains: 2
Atoms: 5,501
Mol. weight: 66.59 kDa
Released: 22 Aug 2018

Explore 6CQP in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6CQP contains 36 α-helices and 21 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.

Chain A: 18 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	197-202	6
α-helix	206-208	3
α-helix	211-213	3
α-helix	214-218	5
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	304-319	16
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	390-404	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

Chain B: 18 helices, 10 β-strands

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
α-helix	284-286	3
β-strand	294-299	6	4
α-helix	306-319	14
β-strand	324-327	4	4
α-helix	334-347	14
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	456-464	9
β-strand	468-472	5	4
α-helix	477-479	3
β-strand	480-482	3	4
α-helix	485-493	9

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Signal recognition particle receptor FtsY	A, B	protein	303	Escherichia coli (strain K12)	P10121 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>6CQP_1 Signal recognition particle receptor FtsY (chains A, B)
GFARLKRSLLKTKENLGSGFISLFRGKKIDDDLFEELEEQLLIADVGVETTRKIITNLTE
GASRKQLRDAEALYGLLKEEMGEILAKVDEPLNVEGKAPFVILMVGVNGVGKTTTIGKLA
RQFEQQGKSVMLAAGDTFRAAAVEQLQVWGQRNNIPVIAQHTGADSASVIFDAIQAAKAR
NIDVLIADTAGRLQNKSHLMEELKKIVRVMKKLDVEAPHEVMLTIDASTGQNAVSQAKLF
HEAVGLTGITLTKLDGTAKGGVIFSVADQFGIPIRYIGVGERIEDLRPFKADDFIEALFA
RED

Primary citation

Discovery of fragments that target key interactions in the signal recognition particle (SRP) as potential leads for a new class of antibiotics. Faoro, C., Wilkinson-White, L., Kwan, A.H. et al. PLoS One (2018) 13:e0200387-e0200387. DOI 10.1371/journal.pone.0200387 · 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
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
5NIY 1.7 Å, Signal recognition particle-docking protein FtsY
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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