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Chlorine in PDB 5y6c: Crystal Structure of Zmasch S128A Mutant Protein From Zymomonas Mobilis

Protein crystallography data

The structure of Crystal Structure of Zmasch S128A Mutant Protein From Zymomonas Mobilis, PDB code: 5y6c was solved by S.-Y.Park, J.-S.Kim, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.83 / 2.40
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 52.149, 52.149, 207.461, 90.00, 90.00, 120.00
R / Rfree (%) 20.6 / 23.5

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Zmasch S128A Mutant Protein From Zymomonas Mobilis (pdb code 5y6c). 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 Zmasch S128A Mutant Protein From Zymomonas Mobilis, PDB code: 5y6c:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in 5y6c

Go back to Chlorine Binding Sites List in 5y6c
Chlorine binding site 1 out of 4 in the Crystal Structure of Zmasch S128A Mutant Protein From Zymomonas Mobilis


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 Zmasch S128A Mutant Protein From Zymomonas Mobilis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl201

b:47.4
occ:1.00
NH1 B:ARG34 3.6 27.0 1.0
OG1 A:THR94 3.7 29.2 1.0
CL A:CL202 4.0 52.2 1.0
N A:GLU95 4.1 25.3 1.0
CD B:ARG34 4.4 25.5 1.0
N A:LYS96 4.4 19.7 1.0
CG A:LYS96 4.5 21.3 1.0
CB A:LYS96 4.7 23.4 1.0
CB A:GLU95 4.7 49.7 1.0
CZ B:ARG34 4.7 38.0 1.0
CA A:GLU95 4.8 30.0 1.0
CG A:GLU95 4.8 42.3 1.0
CA A:THR94 4.9 27.1 1.0
CB A:THR94 4.9 17.1 1.0
CG B:LYS96 5.0 15.1 1.0
C A:THR94 5.0 26.3 1.0

Chlorine binding site 2 out of 4 in 5y6c

Go back to Chlorine Binding Sites List in 5y6c
Chlorine binding site 2 out of 4 in the Crystal Structure of Zmasch S128A Mutant Protein From Zymomonas Mobilis


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 Zmasch S128A Mutant Protein From Zymomonas Mobilis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl202

b:52.2
occ:1.00
NH1 A:ARG34 3.2 27.2 1.0
OG1 B:THR94 3.4 24.7 1.0
N B:GLU95 3.7 24.1 1.0
CL A:CL201 4.0 47.4 1.0
CD A:ARG34 4.1 26.6 1.0
N B:LYS96 4.3 28.5 1.0
CZ A:ARG34 4.4 45.2 1.0
CB B:GLU95 4.4 29.1 1.0
CA B:THR94 4.5 35.7 1.0
CA B:GLU95 4.5 34.4 1.0
CG B:GLU95 4.5 38.5 1.0
CB B:THR94 4.6 19.6 1.0
C B:THR94 4.6 26.0 1.0
CG B:LYS96 4.7 15.1 1.0
NE A:ARG34 4.7 39.3 1.0
C B:GLU95 4.8 25.3 1.0
CB B:LYS96 4.9 34.1 1.0

Chlorine binding site 3 out of 4 in 5y6c

Go back to Chlorine Binding Sites List in 5y6c
Chlorine binding site 3 out of 4 in the Crystal Structure of Zmasch S128A Mutant Protein From Zymomonas Mobilis


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 Zmasch S128A Mutant Protein From Zymomonas Mobilis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl203

b:24.9
occ:1.00
NH2 A:ARG33 3.0 11.7 1.0
O A:HOH315 3.2 14.6 1.0
O B:HOH310 3.3 13.9 1.0
CD A:ARG33 3.4 8.1 1.0
NH2 B:ARG33 3.5 10.3 1.0
CD B:ARG33 3.5 13.2 1.0
NE2 B:GLN127 3.6 31.2 1.0
NE2 A:GLN127 3.7 39.3 1.0
CB B:ARG33 3.9 7.2 1.0
CB A:ARG33 4.0 8.1 1.0
CZ A:ARG33 4.0 18.4 1.0
NE A:ARG33 4.1 17.9 1.0
CG B:ARG33 4.2 14.8 1.0
CG2 B:ILE35 4.2 29.3 1.0
CG A:ARG33 4.2 14.3 1.0
CZ B:ARG33 4.4 16.0 1.0
NE B:ARG33 4.4 19.5 1.0
O B:HOH325 4.6 35.0 1.0
CG2 A:ILE35 4.6 25.9 1.0
O A:HOH322 4.7 18.8 1.0
CD B:GLN127 4.9 49.0 1.0
OH A:TYR90 4.9 22.1 1.0
CD A:GLN127 5.0 47.4 1.0

Chlorine binding site 4 out of 4 in 5y6c

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Chlorine binding site 4 out of 4 in the Crystal Structure of Zmasch S128A Mutant Protein From Zymomonas Mobilis


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 Zmasch S128A Mutant Protein From Zymomonas Mobilis within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl201

b:45.3
occ:1.00
CG B:ARG50 3.4 32.6 1.0
NH2 A:ARG50 3.5 25.1 1.0
OH B:TYR47 3.5 19.8 1.0
NH1 A:ARG50 3.7 24.9 1.0
N B:ARG50 3.8 17.7 1.0
CG B:LYS53 3.9 32.2 1.0
NH1 B:ARG50 4.0 38.4 1.0
CZ A:ARG50 4.1 32.6 1.0
CB B:THR49 4.1 9.6 1.0
CA B:THR49 4.2 20.1 1.0
CD B:ARG50 4.2 34.3 1.0
CG B:PRO125 4.3 36.9 1.0
CE2 B:TYR47 4.4 14.0 1.0
CG2 B:THR49 4.4 16.7 1.0
CZ B:TYR47 4.4 21.0 1.0
C B:THR49 4.4 22.9 1.0
CB B:ARG50 4.6 26.6 1.0
CZ B:ARG50 4.6 50.3 1.0
NE B:ARG50 4.7 43.9 1.0
CA B:ARG50 4.7 26.0 1.0
CD B:LYS53 4.8 37.8 1.0
CB B:PRO125 4.9 22.0 1.0

Reference:

B.N.Kim, M.Shin, S.C.Ha, S.Y.Park, P.W.Seo, A.Hofmann, J.S.Kim. Crystal Structure of An Asch Protein From Zymomonas Mobilis and Its Ribonuclease Activity Specific For Single-Stranded Rna. Sci Rep V. 7 12303 2017.
ISSN: ESSN 2045-2322
PubMed: 28951575
DOI: 10.1038/S41598-017-12186-W
Page generated: Fri Jul 26 21:18:45 2024

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