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Sodium in PDB 5fie: Crystal Structure of N-Terminal Domain of Shaft Pilin Spaa From Lactobacillus Rhamnosus Gg

Protein crystallography data

The structure of Crystal Structure of N-Terminal Domain of Shaft Pilin Spaa From Lactobacillus Rhamnosus Gg, PDB code: 5fie was solved by P.Chaurasia, S.Pratap, I.Von Ossowski, A.Palva, V.Krishnan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 44.31 / 2.00
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 88.615, 88.615, 48.892, 90.00, 90.00, 90.00
R / Rfree (%) 18.5 / 22.2

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of N-Terminal Domain of Shaft Pilin Spaa From Lactobacillus Rhamnosus Gg (pdb code 5fie). 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 Crystal Structure of N-Terminal Domain of Shaft Pilin Spaa From Lactobacillus Rhamnosus Gg, PDB code: 5fie:

Sodium binding site 1 out of 1 in 5fie

Go back to Sodium Binding Sites List in 5fie
Sodium binding site 1 out of 1 in the Crystal Structure of N-Terminal Domain of Shaft Pilin Spaa From Lactobacillus Rhamnosus Gg


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of N-Terminal Domain of Shaft Pilin Spaa From Lactobacillus Rhamnosus Gg within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na201

b:25.9
occ:1.00
O A:THR116 2.3 21.2 1.0
C A:THR116 3.4 19.9 1.0
N A:THR116 3.8 17.4 1.0
CA A:THR116 4.0 19.9 1.0
CB A:THR116 4.2 21.4 1.0
O A:HOH387 4.5 16.3 1.0
N A:GLN117 4.5 16.6 1.0
O A:HOH315 4.5 17.9 1.0
O A:HOH394 4.7 18.3 1.0
O A:HOH402 4.7 19.4 1.0
CA A:GLN117 4.8 18.9 1.0
OE1 A:GLN117 4.8 18.1 1.0
CG2 A:THR116 5.0 25.2 1.0

Reference:

P.Chaurasia, S.Pratap, I.Von Ossowski, A.Palva, V.Krishnan. New Insights About Pilus Formation in Gut-Adapted Lactobacillus Rhamnosus Gg From the Crystal Structure of the Spaa Backbone-Pilin Subunit Sci Rep V. 6 28664 2016.
ISSN: ESSN 2045-2322
PubMed: 27349405
DOI: 10.1038/SREP28664
Page generated: Sun Aug 17 23:49:50 2025

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