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Sodium in PDB 6cvd: High Resolution Crystal Structure of Ftsy-Ng Domain of E. Coli Bound to Fragment 1

Protein crystallography data

The structure of High Resolution Crystal Structure of Ftsy-Ng Domain of E. Coli Bound to Fragment 1, PDB code: 6cvd was solved by C.Faoro, S.F.Ataide, A.Kwan, L.Wilkinson-White, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.01 / 1.78
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 34.341, 76.008, 108.032, 90.00, 90.42, 90.00
R / Rfree (%) 20.2 / 25.2

Sodium Binding Sites:

The binding sites of Sodium atom in the High Resolution Crystal Structure of Ftsy-Ng Domain of E. Coli Bound to Fragment 1 (pdb code 6cvd). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the High Resolution Crystal Structure of Ftsy-Ng Domain of E. Coli Bound to Fragment 1, PDB code: 6cvd:

Sodium binding site 1 out of 1 in 6cvd

Go back to Sodium Binding Sites List in 6cvd
Sodium binding site 1 out of 1 in the High Resolution Crystal Structure of Ftsy-Ng Domain of E. Coli Bound to Fragment 1


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of High Resolution Crystal Structure of Ftsy-Ng Domain of E. Coli Bound to Fragment 1 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Na503

b:30.0
occ:1.00
O B:HOH646 2.3 19.1 1.0
OD1 B:ASP283 2.3 22.5 1.0
O B:PHE483 2.5 17.6 1.0
O B:HOH747 2.7 23.3 1.0
O B:ASP283 2.8 27.2 1.0
C B:ASP283 2.9 27.2 1.0
HA B:ASP283 2.9 42.7 1.0
CG B:ASP283 3.2 22.6 1.0
HG3 B:PRO285 3.2 31.2 1.0
CA B:ASP283 3.4 35.6 1.0
HA B:LYS484 3.5 20.1 1.0
HD3 B:PRO285 3.5 33.6 1.0
N B:GLU284 3.6 25.3 1.0
N B:PRO285 3.7 22.0 1.0
C B:PHE483 3.7 16.0 1.0
HD2 B:PHE483 3.8 17.4 1.0
CB B:ASP283 3.9 23.1 1.0
HA B:PRO285 3.9 22.7 1.0
C B:GLU284 3.9 21.9 1.0
CG B:PRO285 3.9 26.0 1.0
CD B:PRO285 3.9 28.0 1.0
H B:GLU284 4.0 30.4 1.0
HA2 A:GLY195 4.0 31.4 1.0
OD2 B:ASP283 4.1 23.0 1.0
H B:ALA485 4.1 19.3 1.0
HB3 B:PHE483 4.1 17.0 1.0
HB3 B:PRO285 4.1 26.6 1.0
CA B:GLU284 4.1 23.7 1.0
CA B:PRO285 4.2 18.9 1.0
HA B:GLU284 4.3 28.4 1.0
CB B:PRO285 4.4 22.2 1.0
CA B:LYS484 4.4 16.7 1.0
O B:GLU284 4.4 20.4 1.0
HB3 B:ASP283 4.4 27.7 1.0
CD2 B:PHE483 4.4 14.5 1.0
N B:LYS484 4.5 15.7 1.0
O B:HOH619 4.5 19.8 1.0
N A:GLY195 4.6 29.4 1.0
HB2 B:ASP283 4.6 27.7 1.0
O B:ILE468 4.7 15.3 1.0
HG2 B:LYS484 4.7 22.7 1.0
CB B:PHE483 4.7 14.2 1.0
CA B:PHE483 4.7 15.1 1.0
HG2 B:PRO285 4.8 31.2 1.0
CA A:GLY195 4.8 26.2 1.0
N B:ASP283 4.8 20.5 1.0
N B:ALA485 4.9 16.1 1.0
HD2 B:PRO285 4.9 33.6 1.0
CG B:PHE483 4.9 14.7 1.0

Reference:

C.Faoro, L.Wilkinson-White, A.H.Kwan, S.F.Ataide. Discovery of Fragments That Target Key Interactions in the Signal Recognition Particle (Srp) As Potential Leads For A New Class of Antibiotics. Plos One V. 13 00387 2018.
ISSN: ESSN 1932-6203
PubMed: 30044812
DOI: 10.1371/JOURNAL.PONE.0200387
Page generated: Tue Oct 8 06:47:58 2024

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