Chlorine in PDB 5o0x: Crystal Structure of Dehydrogenase Domain of Cylindrospermum Stagnale Nadph-Oxidase 5 (NOX5)

The structure of Crystal Structure of Dehydrogenase Domain of Cylindrospermum Stagnale Nadph-Oxidase 5 (NOX5), PDB code: 5o0x was solved by F.Magnani, S.Nenci, A.Mattevi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	111.09 / 2.20
Space group	P 3 2 1
Cell size a, b, c (Å), α, β, γ (°)	128.279, 128.279, 72.519, 90.00, 90.00, 120.00
R / Rfree (%)	18.4 / 20.9

The binding sites of Chlorine atom in the Crystal Structure of Dehydrogenase Domain of Cylindrospermum Stagnale Nadph-Oxidase 5 (NOX5) (pdb code 5o0x). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 7 binding sites of Chlorine where determined in the Crystal Structure of Dehydrogenase Domain of Cylindrospermum Stagnale Nadph-Oxidase 5 (NOX5), PDB code: 5o0x:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5; 6; 7;

Chlorine binding site 1 out of 7 in the Crystal Structure of Dehydrogenase Domain of Cylindrospermum Stagnale Nadph-Oxidase 5 (NOX5)


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 Dehydrogenase Domain of Cylindrospermum Stagnale Nadph-Oxidase 5 (NOX5) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl802 b:82.3 occ:1.00 NH1 A:ARG478 3.6 39.7 1.0 NH2 A:ARG478 3.8 43.9 1.0 CZ A:ARG478 4.2 40.8 1.0 C15 A:P6G812 4.3 61.6 1.0 C14 A:P6G812 4.7 64.0 1.0

Chlorine binding site 2 out of 7 in the Crystal Structure of Dehydrogenase Domain of Cylindrospermum Stagnale Nadph-Oxidase 5 (NOX5)


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 Dehydrogenase Domain of Cylindrospermum Stagnale Nadph-Oxidase 5 (NOX5) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl803 b:87.7 occ:1.00 O1 A:PEG819 3.6 76.1 1.0 O A:ALA479 3.9 37.0 1.0 N A:GLY481 4.1 30.7 1.0 O A:GLY481 4.2 32.6 1.0 C A:ALA479 4.2 33.1 1.0 C A:VAL480 4.3 31.4 1.0 CA A:GLY485 4.4 34.4 1.0 C2 A:PEG819 4.4 74.1 1.0 CB A:ALA479 4.5 34.6 1.0 N A:VAL480 4.5 33.5 1.0 C1 A:PEG819 4.6 74.3 1.0 CA A:GLY481 4.6 30.9 1.0 CA A:VAL480 4.6 31.9 1.0 C A:GLY481 4.7 32.4 1.0 O2 A:PEG819 4.8 79.6 1.0 O A:VAL480 4.8 34.1 1.0 CA A:ALA479 4.9 33.0 1.0

Chlorine binding site 3 out of 7 in the Crystal Structure of Dehydrogenase Domain of Cylindrospermum Stagnale Nadph-Oxidase 5 (NOX5)


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 Dehydrogenase Domain of Cylindrospermum Stagnale Nadph-Oxidase 5 (NOX5) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl804 b:88.4 occ:1.00 O A:PRO467 3.7 40.6 1.0 NH1 A:ARG434 4.1 40.8 1.0 CA A:PRO470 4.1 57.8 1.0 O A:GLU468 4.2 54.9 1.0 CB A:PRO470 4.4 58.7 1.0 CZ A:ARG434 4.5 39.4 1.0 NH2 A:ARG434 4.6 38.2 1.0 C A:GLU468 4.7 48.1 1.0 N A:PRO470 4.8 59.1 1.0 O A:PRO470 4.8 67.3 1.0 C A:PRO467 4.9 41.6 1.0 O A:MET469 4.9 51.2 1.0 CA A:GLU468 5.0 45.9 1.0 C A:MET469 5.0 50.5 1.0

Chlorine binding site 4 out of 7 in the Crystal Structure of Dehydrogenase Domain of Cylindrospermum Stagnale Nadph-Oxidase 5 (NOX5)


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 Dehydrogenase Domain of Cylindrospermum Stagnale Nadph-Oxidase 5 (NOX5) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl805 b:83.3 occ:1.00 CD A:GLU697 4.1 43.0 1.0 OE1 A:GLU697 4.1 37.3 1.0 OE2 A:GLU697 4.3 41.4 1.0 OG1 A:THR671 4.3 42.0 1.0 CB A:THR671 4.4 38.4 1.0 CG A:GLU697 4.4 37.6 1.0 O A:HOH902 4.7 49.9 1.0 CG2 A:THR671 4.7 39.7 1.0

Chlorine binding site 5 out of 7 in the Crystal Structure of Dehydrogenase Domain of Cylindrospermum Stagnale Nadph-Oxidase 5 (NOX5)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 5 of Crystal Structure of Dehydrogenase Domain of Cylindrospermum Stagnale Nadph-Oxidase 5 (NOX5) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl806 b:0.3 occ:1.00 N3A A:FAD801 3.0 82.7 1.0 C2A A:FAD801 3.3 85.4 1.0 C4A A:FAD801 3.6 73.9 1.0 C14 A:P6G811 3.9 69.0 1.0 N1A A:FAD801 4.1 80.8 1.0 N9A A:FAD801 4.2 68.2 1.0 C15 A:P6G811 4.3 70.0 1.0 O4B A:FAD801 4.5 52.6 1.0 C1B A:FAD801 4.5 58.7 1.0 C5A A:FAD801 4.5 74.1 1.0 C6A A:FAD801 4.7 73.4 1.0

Chlorine binding site 6 out of 7 in the Crystal Structure of Dehydrogenase Domain of Cylindrospermum Stagnale Nadph-Oxidase 5 (NOX5)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 6 of Crystal Structure of Dehydrogenase Domain of Cylindrospermum Stagnale Nadph-Oxidase 5 (NOX5) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl807 b:97.5 occ:1.00 O A:PRO660 3.7 45.2 1.0 OD1 A:ASP661 4.0 56.0 1.0 CG A:PRO660 4.3 42.0 1.0 C A:PRO660 4.3 42.3 1.0 CB A:PRO660 4.5 43.9 1.0 CA A:ASP661 4.7 42.0 1.0 N A:ASP661 4.8 42.5 1.0

Chlorine binding site 7 out of 7 in the Crystal Structure of Dehydrogenase Domain of Cylindrospermum Stagnale Nadph-Oxidase 5 (NOX5)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 7 of Crystal Structure of Dehydrogenase Domain of Cylindrospermum Stagnale Nadph-Oxidase 5 (NOX5) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl808 b:82.2 occ:1.00 OG A:SER482 3.2 46.1 1.0 NZ A:LYS486 3.2 71.8 1.0 O A:HOH990 3.4 66.1 1.0 O A:HOH956 4.1 60.0 1.0 CE A:LYS486 4.1 62.4 1.0 OE1 A:GLU457 4.2 33.4 1.0 CA A:TRP483 4.3 29.9 1.0 CD A:LYS486 4.3 57.3 1.0 N A:TRP483 4.3 29.8 1.0 CB A:TRP483 4.4 30.2 1.0 CB A:SER482 4.4 37.1 1.0 C A:SER482 4.5 31.9 1.0 CD1 A:TRP483 4.6 28.6 1.0 O A:SER482 4.6 32.5 1.0 CD A:GLU457 4.7 34.3 1.0 OE2 A:GLU457 4.7 36.5 1.0 CB A:SER454 4.7 47.8 1.0 CG2 A:ILE453 4.8 52.8 1.0 O A:ILE453 4.8 45.4 1.0 CG A:TRP483 4.9 29.1 1.0

F.Magnani, S.Nenci, E.Millana Fananas, M.Ceccon, E.Romero, M.W.Fraaije, A.Mattevi. Crystal Structures and Atomic Model of Nadph Oxidase. Proc. Natl. Acad. Sci. V. 114 6764 2017U.S.A..
ISSN: ESSN 1091-6490
PubMed: 28607049
DOI: 10.1073/PNAS.1702293114