Chlorine in PDB 8qq5: Structure of Wt Spnox Dh Domain: A Bacterial Nadph Oxidase.

The structure of Structure of Wt Spnox Dh Domain: A Bacterial Nadph Oxidase., PDB code: 8qq5 was solved by M.Thepaut, I.Petit-Hartlein, A.Vermot, A.S.Humm, F.Dupeux, J.A.Marquez, S.Smith, F.Fieschi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.90 / 2.50
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	104.88, 104.88, 139.29, 90, 90, 90
R / Rfree (%)	19.7 / 29

The binding sites of Chlorine atom in the Structure of Wt Spnox Dh Domain: A Bacterial Nadph Oxidase. (pdb code 8qq5). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Structure of Wt Spnox Dh Domain: A Bacterial Nadph Oxidase., PDB code: 8qq5:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Structure of Wt Spnox Dh Domain: A Bacterial Nadph Oxidase.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of Wt Spnox Dh Domain: A Bacterial Nadph Oxidase. within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1001 b:66.3 occ:1.00 OG A:SER374 2.7 62.8 1.0 N A:SER374 3.3 51.7 1.0 CB A:SER374 3.3 61.0 1.0 CG2 A:ILE373 3.8 58.2 1.0 N A:ILE373 3.8 53.7 1.0 CB A:PRO372 3.9 49.1 1.0 CA A:SER374 3.9 60.4 1.0 CG A:LYS398 4.1 86.6 1.0 C A:PRO372 4.2 56.6 1.0 CA A:PRO372 4.2 52.3 1.0 C A:ILE373 4.3 50.6 1.0 O A:PHE397 4.4 79.5 1.0 CA A:ILE373 4.4 52.0 1.0 CB A:ILE373 4.7 57.5 1.0 CA A:LYS398 4.7 101.7 1.0 CD A:LYS398 4.9 94.4 1.0 CB A:LYS398 5.0 103.9 1.0

Chlorine binding site 2 out of 2 in the Structure of Wt Spnox Dh Domain: A Bacterial Nadph Oxidase.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Structure of Wt Spnox Dh Domain: A Bacterial Nadph Oxidase. within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1001 b:54.5 occ:1.00 OG B:SER374 2.9 50.3 1.0 NH1 C:ARG320 3.1 60.7 1.0 N B:SER374 3.3 49.8 1.0 CB B:SER374 3.4 49.6 1.0 CB B:PRO372 3.8 51.8 1.0 N B:ILE373 3.8 49.2 1.0 CG2 B:ILE373 3.9 52.0 1.0 CA B:SER374 3.9 51.5 1.0 CD C:ARG320 4.0 61.6 1.0 CG C:ARG320 4.1 62.0 1.0 C B:PRO372 4.2 47.8 1.0 CG2 C:THR349 4.2 51.1 1.0 CZ C:ARG320 4.2 76.6 1.0 C B:ILE373 4.3 50.8 1.0 CA B:PRO372 4.4 50.8 1.0 CA B:ILE373 4.4 51.2 1.0 C B:PHE399 4.5 109.1 1.0 N B:PHE399 4.5 90.6 1.0 NE C:ARG320 4.5 69.1 1.0 O B:PHE399 4.5 82.6 1.0 O B:PHE397 4.6 75.5 1.0 CB C:ARG320 4.7 59.1 1.0 CB B:ILE373 4.8 52.5 1.0 O B:PRO372 4.8 48.7 1.0 OG C:SER348 5.0 47.8 1.0

I.Petit-Hartlein, A.Vermot, M.Thepaut, A.S.Humm, F.Dupeux, J.Dupuy, V.Chaptal, J.A.Marquez, S.M.E.Smith, F.Fieschi. X-Ray Structure and Enzymatic Study of A Bacterial Nadph Oxidase Highlight the Activation Mechanism of Eukaryotic Nox. Elife V. 13 2024.
ISSN: ESSN 2050-084X
PubMed: 38640072
DOI: 10.7554/ELIFE.93759