Chlorine in PDB 7aqa: Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H382A

All present enzymatic activity of Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H382A:
1.7.2.4;

The structure of Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H382A, PDB code: 7aqa was solved by L.Zhang, E.Bill, P.M.H.Kroneck, O.Einsle, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	62.67 / 1.50
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	68.824, 76.834, 108.513, 90, 93.47, 90
R / Rfree (%)	15.6 / 19.4

The structure of Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H382A also contains other interesting chemical elements:

Calcium	(Ca)	2 atoms
Sodium	(Na)	1 atom
Potassium	(K)	2 atoms
Copper	(Cu)	11 atoms

The binding sites of Chlorine atom in the Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H382A (pdb code 7aqa). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H382A, PDB code: 7aqa:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H382A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H382A within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl706 b:24.1 occ:0.73 O A:HOH1123 3.0 36.7 1.0 NH1 A:ARG181 3.0 19.7 1.0 ND2 A:ASN329 3.3 23.8 1.0 NH2 A:ARG181 3.4 25.9 1.0 N A:CYS328 3.4 19.9 1.0 CZ A:ARG181 3.6 25.9 1.0 CG A:ASN241 3.6 28.8 1.0 CA A:GLY327 3.7 19.4 1.0 CB A:ASN241 3.7 20.3 1.0 ND2 A:ASN241 3.7 33.1 1.0 NE2 A:HIS433 3.8 45.2 1.0 O A:CYS328 4.0 21.1 1.0 CG A:ASN329 4.1 22.5 1.0 C A:GLY327 4.1 18.4 1.0 OD1 A:ASN329 4.2 21.6 1.0 OD1 A:ASN241 4.2 34.0 1.0 CD2 A:HIS433 4.3 41.6 1.0 C A:CYS328 4.3 20.4 1.0 O A:HOH1180 4.4 22.4 1.0 CA A:CYS328 4.5 22.8 1.0 CE1 A:HIS433 4.6 43.9 1.0 N A:GLY327 4.9 20.1 1.0 NE A:ARG181 5.0 22.1 1.0

Chlorine binding site 2 out of 3 in the Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H382A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H382A within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl707 b:31.7 occ:0.76 O A:HOH1245 2.4 43.3 1.0 O A:HOH812 2.9 45.5 1.0 NZ A:LYS403 3.2 29.2 1.0 NH2 A:ARG388 3.2 28.7 1.0 NE A:ARG388 3.4 26.2 1.0 ND2 A:ASN390 3.5 22.6 1.0 CZ A:ARG388 3.8 24.5 1.0 CE A:LYS403 3.8 26.3 1.0 OD1 A:ASP479 4.1 56.4 1.0 O A:HOH1238 4.2 35.9 1.0 O A:GLY478 4.2 28.2 1.0 CA A:ASP479 4.2 30.6 1.0 OD2 A:ASP386 4.5 23.8 1.0 O A:HOH986 4.6 41.4 1.0 CD A:ARG388 4.6 24.5 1.0 CG A:ASN390 4.6 26.9 1.0 C A:GLY478 4.7 27.2 1.0 O A:HOH1026 4.8 24.7 1.0 O A:ASP479 4.8 35.6 1.0 N A:ASP479 4.8 31.5 1.0 C A:ASP479 5.0 31.5 1.0 CB A:ASP479 5.0 34.0 1.0 CG A:ASP479 5.0 50.5 1.0

Chlorine binding site 3 out of 3 in the Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H382A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H382A within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl707 b:24.9 occ:0.77 O B:HOH1134 2.9 38.8 1.0 NH1 B:ARG181 3.2 27.1 1.0 N B:CYS328 3.4 24.2 1.0 ND2 B:ASN329 3.4 30.9 1.0 CA B:GLY327 3.5 23.4 1.0 CB B:ASN241 3.6 19.8 1.0 NH2 B:ARG181 3.6 29.8 1.0 CG B:ASN241 3.6 27.8 1.0 ND2 B:ASN241 3.7 31.5 1.0 O B:CYS328 3.8 26.6 1.0 CZ B:ARG181 3.8 30.3 1.0 O B:HOH1103 3.8 39.6 1.0 NE2 B:HIS433 3.9 47.7 1.0 C B:GLY327 4.0 26.8 1.0 OD1 B:ASN329 4.0 31.6 1.0 CG B:ASN329 4.1 28.3 1.0 C B:CYS328 4.3 23.6 1.0 OD1 B:ASN241 4.3 38.5 1.0 CE1 B:HIS433 4.4 45.9 1.0 CA B:CYS328 4.4 24.1 1.0 O B:HOH1093 4.5 21.9 1.0 CD2 B:HIS433 4.5 47.3 1.0 N B:GLY327 4.7 23.9 1.0 CB B:CYS328 5.0 27.5 1.0 CA B:ASN241 5.0 22.5 1.0

L.Zhang, E.Bill, P.M.H.Kroneck, O.Einsle. A [3CU:2S] Cluster Provides Insight Into the Assembly and Function of the Cuz Site of Nitrous Oxide Reductase Chem Sci 2021.
ISSN: ESSN 2041-6539
DOI: 10.1039/D0SC05204C