Chlorine in PDB 1nza: Divalent Cation Tolerance Protein (Cut A1) From Thermus Thermophilus HB8

The structure of Divalent Cation Tolerance Protein (Cut A1) From Thermus Thermophilus HB8, PDB code: 1nza was solved by B.Bagautdinov, M.Miyano, T.H.Tahirov, Riken Structuralgenomics/Proteomics Initiative (Rsgi), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.00 / 1.70
Space group	I 2 3
Cell size a, b, c (Å), α, β, γ (°)	83.003, 83.003, 83.003, 90.00, 90.00, 90.00
R / Rfree (%)	22.9 / 24.6

The structure of Divalent Cation Tolerance Protein (Cut A1) From Thermus Thermophilus HB8 also contains other interesting chemical elements:

Sodium

(Na)

2 atoms

The binding sites of Chlorine atom in the Divalent Cation Tolerance Protein (Cut A1) From Thermus Thermophilus HB8 (pdb code 1nza). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Divalent Cation Tolerance Protein (Cut A1) From Thermus Thermophilus HB8, PDB code: 1nza:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the Divalent Cation Tolerance Protein (Cut A1) From Thermus Thermophilus HB8


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Divalent Cation Tolerance Protein (Cut A1) From Thermus Thermophilus HB8 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl108 b:28.1 occ:1.00 O A:HOH509 2.8 24.0 1.0 N A:GLY36 3.1 15.9 1.0 CB A:PRO35 3.8 18.3 1.0 CA A:GLY36 3.8 14.3 1.0 O1 A:GOL500 3.8 43.7 1.0 CG A:LEU53 3.9 14.1 1.0 CD1 A:LEU53 4.0 13.9 1.0 O2 A:GOL500 4.1 46.1 1.0 C A:PRO35 4.1 15.2 1.0 CA A:PRO35 4.1 16.1 1.0 CD2 A:LEU53 4.2 12.9 1.0 O A:GLU52 4.5 13.6 1.0 O A:HOH568 4.8 44.3 1.0 C1 A:GOL500 4.9 44.9 1.0 C A:GLY36 5.0 14.1 1.0

Chlorine binding site 2 out of 4 in the Divalent Cation Tolerance Protein (Cut A1) From Thermus Thermophilus HB8


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Divalent Cation Tolerance Protein (Cut A1) From Thermus Thermophilus HB8 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl109 b:39.3 occ:1.00 NA A:NA104 3.3 14.6 1.0 N A:GLU81 3.7 20.9 1.0 O A:HOH518 3.8 36.9 1.0 OE2 A:GLU52 3.9 23.2 1.0 OG1 A:THR8 3.9 16.2 1.0 CA A:PRO80 4.1 24.5 1.0 O A:THR8 4.2 16.3 1.0 O A:HOH510 4.3 29.4 1.0 CE1 A:HIS75 4.3 24.5 1.0 NE2 A:HIS75 4.3 21.8 1.0 CB A:GLU81 4.4 22.3 1.0 C A:PRO80 4.4 24.1 1.0 O A:HOH584 4.4 40.0 1.0 O A:VAL79 4.4 26.3 1.0 O A:HOH512 4.5 24.6 1.0 CD1 A:TYR77 4.6 31.1 1.0 CA A:GLU81 4.7 20.9 1.0 CB A:PRO80 4.9 25.4 1.0 C A:THR8 4.9 16.8 1.0 CD A:GLU52 5.0 19.0 1.0

Chlorine binding site 3 out of 4 in the Divalent Cation Tolerance Protein (Cut A1) From Thermus Thermophilus HB8


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Divalent Cation Tolerance Protein (Cut A1) From Thermus Thermophilus HB8 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl110 b:33.0 occ:1.00 O3 A:GOL500 2.8 46.9 1.0 O A:HOH517 3.1 29.4 1.0 CG A:GLN51 3.8 12.0 1.0 CD A:GLN51 3.8 14.2 1.0 C3 A:GOL500 4.1 46.2 1.0 OE1 A:GLN51 4.1 15.9 1.0 NE2 A:GLN51 4.1 16.3 1.0 OE2 A:GLU49 4.3 32.7 1.0

Chlorine binding site 4 out of 4 in the Divalent Cation Tolerance Protein (Cut A1) From Thermus Thermophilus HB8


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Divalent Cation Tolerance Protein (Cut A1) From Thermus Thermophilus HB8 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl111 b:49.2 occ:1.00 N A:GLN44 3.6 44.3 1.0 CD1 A:TRP43 3.8 44.4 1.0 CA A:TRP43 3.9 40.2 1.0 O A:HOH546 4.2 56.3 1.0 O A:ARG42 4.2 33.0 1.0 C A:TRP43 4.3 41.6 1.0 CG A:TRP43 4.6 44.0 1.0 NE1 A:TRP43 4.6 46.0 1.0 CA A:GLN44 4.6 45.2 1.0 N A:TRP43 4.7 36.0 1.0 C A:ARG42 4.8 32.7 1.0 CB A:TRP43 4.8 41.5 1.0 CD A:GLN44 4.9 51.4 1.0

B.Bagautdinov, B.Bagautdinov, M.Miyano, T.H.Tahirov, Riken Structuralgenomics/Proteomics Initiative (Rsgi). N/A N/A.
ISSN: ESSN 1744-3091
PubMed: 24699729
DOI: 10.1107/S2053230X14003422