Chlorine in PDB 6rl0: Recombinant Pseudomonas Stutzeri Nitrous Oxide Reductase, Form I

All present enzymatic activity of Recombinant Pseudomonas Stutzeri Nitrous Oxide Reductase, Form I:
1.7.2.4;

The structure of Recombinant Pseudomonas Stutzeri Nitrous Oxide Reductase, Form I, PDB code: 6rl0 was solved by L.Zhang, A.Wuest, B.Prasser, C.Mueller, O.Einsle, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.91 / 1.78
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	108.916, 73.372, 136.342, 90.00, 95.07, 90.00
R / Rfree (%)	15.7 / 19.2

The structure of Recombinant Pseudomonas Stutzeri Nitrous Oxide Reductase, Form I also contains other interesting chemical elements:

Potassium	(K)	4 atoms
Calcium	(Ca)	4 atoms
Copper	(Cu)	24 atoms
Sodium	(Na)	4 atoms

The binding sites of Chlorine atom in the Recombinant Pseudomonas Stutzeri Nitrous Oxide Reductase, Form I (pdb code 6rl0). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Recombinant Pseudomonas Stutzeri Nitrous Oxide Reductase, Form I, PDB code: 6rl0:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the Recombinant Pseudomonas Stutzeri Nitrous Oxide Reductase, Form I


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Recombinant Pseudomonas Stutzeri Nitrous Oxide Reductase, Form I within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl702 b:22.8 occ:0.68 CE1 A:HIS382 2.8 20.2 0.5 ND1 A:HIS382 3.0 22.1 0.5 O A:HOH1075 3.1 34.6 1.0 NH1 A:ARG181 3.1 30.5 1.0 ND1 A:HIS382 3.3 21.1 0.5 N A:CYS328 3.3 21.9 1.0 ND2 A:ASN329 3.4 23.1 1.0 CE1 A:HIS382 3.4 21.2 0.5 NH2 A:ARG181 3.5 29.1 1.0 CB A:ASN241 3.6 21.1 1.0 CA A:GLY327 3.7 23.0 1.0 O A:CYS328 3.7 23.8 1.0 CZ A:ARG181 3.7 30.2 1.0 CG A:ASN241 3.7 25.7 1.0 CG A:ASN329 3.9 23.0 1.0 OD1 A:ASN329 3.9 21.0 1.0 C A:GLY327 4.0 21.7 1.0 C A:CYS328 4.1 23.6 1.0 NE2 A:HIS382 4.1 18.9 0.5 OD1 A:ASN241 4.2 31.5 1.0 CE1 A:HIS433 4.2 33.0 1.0 ND2 A:ASN241 4.2 27.4 1.0 CA A:CYS328 4.3 22.4 1.0 CG A:HIS382 4.3 20.1 0.5 O A:HOH1122 4.3 20.3 1.0 CG A:HIS382 4.6 20.6 0.5 NE2 A:HIS382 4.7 21.7 0.5 ND1 A:HIS433 4.7 29.4 1.0 CB A:CYS328 4.8 24.3 1.0 CD2 A:HIS382 4.9 21.1 0.5 N A:ASN329 4.9 20.4 1.0 N A:GLY327 4.9 21.5 1.0 CA A:ASN241 5.0 19.4 1.0

Chlorine binding site 2 out of 4 in the Recombinant Pseudomonas Stutzeri Nitrous Oxide Reductase, Form I


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Recombinant Pseudomonas Stutzeri Nitrous Oxide Reductase, Form I within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl702 b:28.1 occ:0.84 CD2 B:HIS382 3.0 25.2 0.5 NE2 B:HIS382 3.0 25.2 0.5 NH1 B:ARG181 3.1 33.1 1.0 O B:HOH1026 3.2 39.2 1.0 ND1 B:HIS382 3.3 21.1 0.5 N B:CYS328 3.3 20.3 1.0 ND2 B:ASN329 3.3 24.9 1.0 CE1 B:HIS382 3.4 21.9 0.5 NH2 B:ARG181 3.5 34.1 1.0 CA B:GLY327 3.6 22.6 1.0 CB B:ASN241 3.6 25.6 1.0 O B:CYS328 3.7 22.0 1.0 CZ B:ARG181 3.8 32.7 1.0 CG B:ASN241 3.8 26.4 1.0 CG B:ASN329 3.9 25.7 1.0 OD1 B:ASN329 3.9 24.7 1.0 C B:GLY327 4.0 21.1 1.0 C B:CYS328 4.0 24.9 1.0 OD1 B:ASN241 4.2 38.2 1.0 CE1 B:HIS433 4.2 36.6 1.0 CA B:CYS328 4.3 22.7 1.0 ND2 B:ASN241 4.3 28.1 1.0 CE1 B:HIS382 4.3 24.7 0.5 CG B:HIS382 4.3 24.8 0.5 O B:HOH1066 4.5 23.8 1.0 CG B:HIS382 4.6 20.6 0.5 NE2 B:HIS382 4.7 22.8 0.5 ND1 B:HIS433 4.7 34.7 1.0 CB B:CYS328 4.8 24.1 1.0 N B:ASN329 4.8 21.3 1.0 N B:GLY327 4.9 21.1 1.0 ND1 B:HIS382 5.0 24.7 0.5

Chlorine binding site 3 out of 4 in the Recombinant Pseudomonas Stutzeri Nitrous Oxide Reductase, Form I


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Recombinant Pseudomonas Stutzeri Nitrous Oxide Reductase, Form I within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl702 b:26.3 occ:0.72 CE1 C:HIS382 2.9 20.0 0.5 ND1 C:HIS382 3.1 20.9 0.5 O C:HOH1040 3.1 42.5 1.0 NH1 C:ARG181 3.2 30.0 1.0 N C:CYS328 3.2 22.8 1.0 ND1 C:HIS382 3.2 16.1 0.5 ND2 C:ASN329 3.4 22.6 1.0 CE1 C:HIS382 3.5 17.1 0.5 NH2 C:ARG181 3.5 34.5 1.0 CB C:ASN241 3.6 22.4 1.0 O C:CYS328 3.6 23.9 1.0 CA C:GLY327 3.6 21.5 1.0 CG C:ASN241 3.7 28.8 1.0 CZ C:ARG181 3.8 32.7 1.0 OD1 C:ASN329 3.8 22.6 1.0 CG C:ASN329 3.9 23.5 1.0 C C:GLY327 3.9 23.3 1.0 C C:CYS328 4.0 22.1 1.0 OD1 C:ASN241 4.1 33.9 1.0 CE1 C:HIS433 4.2 39.6 1.0 NE2 C:HIS382 4.2 20.3 0.5 CA C:CYS328 4.2 22.4 1.0 ND2 C:ASN241 4.2 31.7 1.0 O C:HOH1075 4.4 23.4 1.0 CG C:HIS382 4.4 20.3 0.5 CG C:HIS382 4.5 17.3 0.5 ND1 C:HIS433 4.7 34.6 1.0 CB C:CYS328 4.8 21.4 1.0 NE2 C:HIS382 4.8 17.2 0.5 N C:ASN329 4.8 20.2 1.0 N C:GLY327 4.9 20.2 1.0 CD2 C:HIS382 5.0 20.3 0.5 CA C:ASN241 5.0 20.1 1.0

Chlorine binding site 4 out of 4 in the Recombinant Pseudomonas Stutzeri Nitrous Oxide Reductase, Form I


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Recombinant Pseudomonas Stutzeri Nitrous Oxide Reductase, Form I within 5.0Å range: probe atom residue distance (Å) B Occ D:Cl702 b:26.7 occ:0.71 O D:HOH1039 3.1 36.5 1.0 CD2 D:HIS382 3.1 21.4 0.5 NE2 D:HIS382 3.1 21.2 0.5 NH1 D:ARG181 3.2 35.6 1.0 N D:CYS328 3.3 23.8 1.0 CD2 D:HIS382 3.4 19.6 0.6 ND2 D:ASN329 3.4 25.1 1.0 NH2 D:ARG181 3.5 39.4 1.0 CB D:ASN241 3.5 25.3 1.0 CA D:GLY327 3.6 22.2 1.0 O D:CYS328 3.7 26.3 1.0 CG D:ASN241 3.7 29.0 1.0 CZ D:ARG181 3.8 37.8 1.0 NE2 D:HIS382 3.9 23.8 0.6 OD1 D:ASN241 3.9 36.7 1.0 CG D:ASN329 4.0 23.6 1.0 OD1 D:ASN329 4.0 22.2 1.0 C D:GLY327 4.0 23.2 1.0 C D:CYS328 4.1 24.7 1.0 CE1 D:HIS433 4.2 32.6 1.0 CA D:CYS328 4.2 24.3 1.0 ND2 D:ASN241 4.3 27.0 1.0 CG D:HIS382 4.4 22.2 0.5 O D:HOH1027 4.4 24.4 1.0 CE1 D:HIS382 4.4 22.2 0.5 CG D:HIS382 4.6 21.4 0.6 ND1 D:HIS433 4.7 31.3 1.0 CB D:CYS328 4.7 25.9 1.0 N D:ASN329 4.9 22.9 1.0 N D:GLY327 4.9 21.6 1.0 CA D:ASN241 4.9 22.2 1.0 O D:HIS326 5.0 22.9 1.0

L.Zhang, A.Wust, B.Prasser, C.Muller, O.Einsle. Functional Assembly of Nitrous Oxide Reductase Provides Insights Into Copper Site Maturation. Proc.Natl.Acad.Sci.Usa V. 116 12822 2019.
ISSN: ESSN 1091-6490
PubMed: 31189605
DOI: 10.1073/PNAS.1903819116