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Chlorine in PDB 5yxg: Crystal Structure of C-Terminal Fragment of Spad From Lactobacillus Rhamnosus Gg Generated By Limited Proteolysis

Protein crystallography data

The structure of Crystal Structure of C-Terminal Fragment of Spad From Lactobacillus Rhamnosus Gg Generated By Limited Proteolysis, PDB code: 5yxg was solved by P.Chaurasia, S.Pratap, A.Palva, I.Von Ossowski, V.Krishnan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 72.66 / 1.48
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 50.106, 83.160, 149.403, 90.00, 90.00, 90.00
R / Rfree (%) 17.7 / 19.5

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of C-Terminal Fragment of Spad From Lactobacillus Rhamnosus Gg Generated By Limited Proteolysis (pdb code 5yxg). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Crystal Structure of C-Terminal Fragment of Spad From Lactobacillus Rhamnosus Gg Generated By Limited Proteolysis, PDB code: 5yxg:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in 5yxg

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Chlorine binding site 1 out of 4 in the Crystal Structure of C-Terminal Fragment of Spad From Lactobacillus Rhamnosus Gg Generated By Limited Proteolysis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of C-Terminal Fragment of Spad From Lactobacillus Rhamnosus Gg Generated By Limited Proteolysis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl501

b:17.4
occ:0.94
O A:HOH910 2.9 40.4 1.0
O B:HOH606 3.0 22.7 1.0
OG1 A:THR442 3.1 12.3 1.0
NE2 A:GLN382 3.1 14.8 1.0
CA A:ARG383 3.6 11.5 1.0
C A:ARG383 3.6 12.4 1.0
CG A:GLN382 3.7 12.3 1.0
CG A:MET384 3.8 16.4 1.0
N A:MET384 3.8 13.8 1.0
CB A:THR442 3.8 11.5 1.0
CD A:GLN382 3.9 12.6 1.0
N A:ARG383 3.9 11.1 1.0
C A:GLN382 3.9 10.4 1.0
O A:GLN382 3.9 10.6 1.0
O A:ARG383 4.1 11.6 1.0
N A:THR442 4.1 10.4 1.0
OD2 B:ASP200 4.1 19.0 1.0
CB A:GLN382 4.3 11.1 1.0
O A:HOH777 4.3 25.6 1.0
O A:HOH651 4.4 17.1 1.0
C A:TYR441 4.5 10.5 1.0
SD A:MET384 4.6 19.7 1.0
CA A:THR442 4.6 10.7 1.0
CB A:MET384 4.7 16.2 1.0
CA A:MET384 4.8 15.2 1.0
CA A:GLN382 4.8 10.8 1.0
CA A:TYR441 4.9 10.7 1.0
CB A:ARG383 5.0 12.2 1.0

Chlorine binding site 2 out of 4 in 5yxg

Go back to Chlorine Binding Sites List in 5yxg
Chlorine binding site 2 out of 4 in the Crystal Structure of C-Terminal Fragment of Spad From Lactobacillus Rhamnosus Gg Generated By Limited Proteolysis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of C-Terminal Fragment of Spad From Lactobacillus Rhamnosus Gg Generated By Limited Proteolysis within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl501

b:25.9
occ:0.95
OG1 B:THR442 3.0 10.8 1.0
NE2 B:GLN382 3.1 16.7 1.0
O B:HOH946 3.4 34.5 1.0
C B:ARG383 3.7 12.3 1.0
CG B:MET384 3.7 17.1 1.0
N B:MET384 3.7 13.0 1.0
CB B:THR442 3.7 10.2 1.0
CA B:ARG383 3.7 11.8 1.0
CG B:GLN382 3.8 13.7 1.0
O B:HOH620 3.9 21.0 1.0
N B:THR442 4.0 10.2 1.0
CD B:GLN382 4.0 15.1 1.0
O B:GLN382 4.1 10.4 1.0
N B:ARG383 4.1 10.7 1.0
C B:GLN382 4.1 11.1 1.0
O B:ARG383 4.2 12.0 1.0
C B:TYR441 4.3 10.7 1.0
CB B:GLN382 4.5 12.6 1.0
CA B:THR442 4.5 10.0 1.0
CB B:MET384 4.5 16.1 1.0
SD B:MET384 4.5 18.9 1.0
CA B:MET384 4.6 14.9 1.0
CA B:TYR441 4.7 11.0 1.0
O B:TYR441 4.9 11.3 1.0
CG2 B:THR442 4.9 10.6 1.0
CA B:GLN382 5.0 11.1 1.0

Chlorine binding site 3 out of 4 in 5yxg

Go back to Chlorine Binding Sites List in 5yxg
Chlorine binding site 3 out of 4 in the Crystal Structure of C-Terminal Fragment of Spad From Lactobacillus Rhamnosus Gg Generated By Limited Proteolysis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of C-Terminal Fragment of Spad From Lactobacillus Rhamnosus Gg Generated By Limited Proteolysis within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl502

b:20.5
occ:0.85
O B:HOH859 3.0 20.1 1.0
N B:ASP303 3.5 14.9 1.0
CD B:PRO302 3.5 14.6 1.0
CG B:ASP303 3.6 17.7 1.0
CB B:ASP303 3.7 16.3 1.0
CG B:PRO302 3.7 14.7 1.0
OD2 B:ASP303 3.8 20.6 1.0
N B:PRO302 3.9 14.1 1.0
OD1 B:ASP303 4.1 18.4 1.0
C B:ASP301 4.2 15.0 1.0
CA B:ASP301 4.2 16.1 1.0
CA B:ASP303 4.2 15.4 1.0
O B:THR300 4.5 15.8 1.0
C B:PRO302 4.5 14.7 1.0
CA B:PRO302 4.6 14.1 1.0
CB B:PRO302 4.7 14.4 1.0
O B:HOH638 5.0 40.5 1.0

Chlorine binding site 4 out of 4 in 5yxg

Go back to Chlorine Binding Sites List in 5yxg
Chlorine binding site 4 out of 4 in the Crystal Structure of C-Terminal Fragment of Spad From Lactobacillus Rhamnosus Gg Generated By Limited Proteolysis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Crystal Structure of C-Terminal Fragment of Spad From Lactobacillus Rhamnosus Gg Generated By Limited Proteolysis within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl503

b:19.9
occ:1.00
O B:HOH840 2.9 24.6 1.0
N B:PHE238 3.1 14.8 1.0
CB B:ASP295 3.3 19.8 1.0
N B:LEU297 3.3 15.7 1.0
N B:GLY298 3.5 15.1 1.0
CA B:ASP295 3.6 17.4 1.0
CA B:GLN237 3.6 17.5 1.0
C B:ASP295 3.6 15.9 1.0
C B:LEU297 3.7 15.9 1.0
O B:PHE238 3.7 14.1 1.0
N B:PHE296 3.7 15.1 1.0
CA B:LEU297 3.8 15.8 1.0
C B:GLN237 3.9 14.9 1.0
C B:PHE238 3.9 13.2 1.0
CB B:LEU297 3.9 16.7 1.0
CG B:GLN237 4.0 24.8 1.0
CA B:PHE238 4.1 14.0 1.0
O B:ASP295 4.2 16.1 1.0
CA B:GLY298 4.2 15.2 1.0
CB B:GLN237 4.2 20.2 1.0
CG B:ASP295 4.4 23.6 1.0
N B:LYS239 4.4 13.7 1.0
O B:LEU297 4.4 16.6 1.0
C B:PHE296 4.4 15.7 1.0
OD1 B:ASP295 4.5 25.2 1.0
O B:ASN236 4.5 15.7 1.0
O B:HOH903 4.5 37.5 1.0
CA B:PHE296 4.6 15.2 1.0
CA B:LYS239 4.7 13.7 1.0
CG B:LEU297 4.7 16.6 1.0
N B:GLN237 4.7 16.1 1.0
CB B:LYS239 4.8 14.8 1.0
CB B:PHE238 4.9 13.6 1.0

Reference:

P.Chaurasia, S.Pratap, A.Palva, I.Von Ossowski, V.Krishnan. Bent Conformation of A Backbone Pilin N-Terminal Domain Supports A Three-Stage Pilus Assembly Mechanism. Commun Biol V. 1 94 2018.
ISSN: ESSN 2399-3642
PubMed: 30271975
DOI: 10.1038/S42003-018-0100-0
Page generated: Fri Jul 26 21:35:42 2024

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