Bromine in PDB 8qq1: Spnox Dehydrogenase Domain, Mutant F397W in Complex with Flavin Adenine Dinucleotide (Fad)

The structure of Spnox Dehydrogenase Domain, Mutant F397W in Complex with Flavin Adenine Dinucleotide (Fad), PDB code: 8qq1 was solved by A.S.Humm, F.Dupeux, A.Vermot, I.Petit-Harleim, F.Fieschi, J.A.Marquez, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.99 / 1.94
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	104.622, 104.622, 142.688, 90, 90, 90
R / Rfree (%)	19 / 22.5

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20; Page 3, Binding sites: 21 - 26;

Binding sites:

The binding sites of Bromine atom in the Spnox Dehydrogenase Domain, Mutant F397W in Complex with Flavin Adenine Dinucleotide (Fad) (pdb code 8qq1). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 26 binding sites of Bromine where determined in the Spnox Dehydrogenase Domain, Mutant F397W in Complex with Flavin Adenine Dinucleotide (Fad), PDB code: 8qq1:
Jump to Bromine binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Bromine binding site 1 out of 26 in the Spnox Dehydrogenase Domain, Mutant F397W in Complex with Flavin Adenine Dinucleotide (Fad)


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Spnox Dehydrogenase Domain, Mutant F397W in Complex with Flavin Adenine Dinucleotide (Fad) within 5.0Å range: probe atom residue distance (Å) B Occ C:Br802 b:40.8 occ:0.40 O C:HOH990 2.9 26.5 1.0 N C:SER215 3.2 26.1 1.0 OG C:SER215 3.7 29.1 1.0 CB C:SER215 3.9 27.6 1.0 CA C:GLN214 3.9 26.7 1.0 CE1 C:HIS306 3.9 33.8 1.0 O C:HOH1047 3.9 53.1 1.0 C C:GLN214 4.0 26.0 1.0 CA C:SER215 4.1 25.8 1.0 CB C:GLN214 4.2 28.4 1.0 CB C:GLU281 4.2 33.5 1.0 NE2 C:HIS306 4.4 33.8 1.0 CG C:GLN214 4.6 33.9 1.0 CD2 C:TYR302 4.6 28.3 1.0 CE2 C:TYR302 4.7 29.0 1.0 O C:SER215 4.9 25.3 1.0

Bromine binding site 2 out of 26 in the Spnox Dehydrogenase Domain, Mutant F397W in Complex with Flavin Adenine Dinucleotide (Fad)


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of Spnox Dehydrogenase Domain, Mutant F397W in Complex with Flavin Adenine Dinucleotide (Fad) within 5.0Å range: probe atom residue distance (Å) B Occ C:Br803 b:49.0 occ:0.57 O C:HOH1031 3.0 52.9 1.0 O C:HOH936 3.1 48.1 1.0 CA C:GLY240 3.7 27.7 1.0 N C:HIS241 3.7 29.7 1.0 CE1 C:HIS241 3.7 42.9 1.0 CB C:THR244 3.8 31.1 1.0 CG2 C:THR244 3.8 31.8 1.0 ND1 C:HIS241 3.8 41.8 1.0 NE2 C:HIS241 4.0 43.0 1.0 C C:GLY240 4.1 29.4 1.0 CG C:HIS241 4.2 38.8 1.0 O C:HIS241 4.3 31.2 1.0 CD2 C:HIS241 4.3 41.3 1.0 CE1 C:TYR246 4.3 32.9 1.0 OG1 C:THR244 4.4 32.6 1.0 N C:GLY240 4.5 26.0 1.0 CA C:HIS241 4.7 31.6 1.0 O C:THR244 4.9 26.5 1.0 OE2 C:GLU305 4.9 46.4 1.0 CB C:HIS241 5.0 33.9 1.0 C C:HIS241 5.0 31.6 1.0 CA C:THR244 5.0 28.5 1.0

Bromine binding site 3 out of 26 in the Spnox Dehydrogenase Domain, Mutant F397W in Complex with Flavin Adenine Dinucleotide (Fad)


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 3 of Spnox Dehydrogenase Domain, Mutant F397W in Complex with Flavin Adenine Dinucleotide (Fad) within 5.0Å range: probe atom residue distance (Å) B Occ C:Br804 b:48.0 occ:0.45 N C:GLY276 3.2 31.4 1.0 CA C:TYR275 3.7 31.3 1.0 NH1 C:ARG273 3.8 50.5 1.0 C C:TYR275 3.9 30.7 1.0 CE1 C:HIS277 4.0 51.7 1.0 NE2 C:HIS277 4.1 51.7 1.0 CD2 C:TYR275 4.1 38.3 1.0 CB C:TYR275 4.1 32.4 1.0 CA C:GLY276 4.2 32.4 1.0 NH2 C:ARG273 4.3 54.4 1.0 C C:GLY276 4.4 33.4 1.0 O C:GLY276 4.4 33.4 1.0 CG C:TYR275 4.5 35.5 1.0 CZ C:ARG273 4.5 53.1 1.0 ND1 C:HIS277 4.7 50.6 1.0 O C:HOH1084 4.7 49.6 1.0 CD2 C:HIS277 4.8 50.0 1.0 O C:ALA274 4.9 31.9 1.0 N C:TYR275 5.0 30.3 1.0

Bromine binding site 4 out of 26 in the Spnox Dehydrogenase Domain, Mutant F397W in Complex with Flavin Adenine Dinucleotide (Fad)


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 4 of Spnox Dehydrogenase Domain, Mutant F397W in Complex with Flavin Adenine Dinucleotide (Fad) within 5.0Å range: probe atom residue distance (Å) B Occ C:Br805 b:38.9 occ:0.57 N C:ARG320 3.2 32.1 1.0 O C:HOH1022 3.2 43.6 1.0 O C:HOH1012 3.6 42.6 1.0 CA C:GLY293 3.7 25.4 1.0 CB C:ASN324 3.7 34.2 1.0 CA C:PHE319 3.8 30.3 1.0 CB C:ARG320 3.9 37.6 1.0 C C:PHE319 3.9 31.2 1.0 CA C:ARG320 4.1 33.9 1.0 CG C:ARG320 4.1 45.3 1.0 CB C:PHE319 4.2 30.0 1.0 O C:HOH911 4.2 31.9 1.0 CD C:ARG320 4.3 52.1 1.0 O C:ASN324 4.4 33.0 1.0 N C:GLY293 4.4 25.3 1.0 CG C:ASN324 4.4 37.7 1.0 O C:HOH985 4.7 48.0 1.0 O C:SER318 4.8 29.1 1.0 NZ C:LYS250 4.8 46.2 1.0 C C:GLY293 4.9 25.2 1.0 C C:ASN324 4.9 32.2 1.0 ND2 C:ASN324 4.9 38.0 1.0 CA C:ASN324 4.9 33.2 1.0 OD1 C:ASN324 5.0 40.0 1.0 C C:ARG320 5.0 33.5 1.0

Bromine binding site 5 out of 26 in the Spnox Dehydrogenase Domain, Mutant F397W in Complex with Flavin Adenine Dinucleotide (Fad)


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 5 of Spnox Dehydrogenase Domain, Mutant F397W in Complex with Flavin Adenine Dinucleotide (Fad) within 5.0Å range: probe atom residue distance (Å) B Occ C:Br806 b:36.1 occ:0.44 O C:HOH981 2.9 46.0 1.0 O C:HOH997 3.4 44.9 1.0 N C:LEU330 3.4 30.5 1.0 CA C:TYR327 3.5 27.8 1.0 CB C:LEU330 3.8 30.5 1.0 C C:TYR327 3.8 28.8 1.0 CB C:ASP329 3.8 38.5 1.0 N C:ASP329 3.9 31.0 1.0 O C:TYR327 4.1 29.5 1.0 O C:HOH999 4.2 43.9 1.0 CA C:ASP329 4.2 33.1 1.0 CA C:LEU330 4.2 30.1 1.0 CD1 C:TYR327 4.2 27.7 1.0 C C:ASP329 4.2 32.0 1.0 N C:TYR327 4.3 27.7 1.0 N C:LEU328 4.3 29.0 1.0 CB C:TYR327 4.4 27.1 1.0 CG C:TYR327 4.8 27.1 1.0 C C:LEU328 4.8 30.3 1.0 NZ C:LYS194 4.9 56.5 1.0 CG C:ASP329 4.9 50.1 1.0

Bromine binding site 6 out of 26 in the Spnox Dehydrogenase Domain, Mutant F397W in Complex with Flavin Adenine Dinucleotide (Fad)


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 6 of Spnox Dehydrogenase Domain, Mutant F397W in Complex with Flavin Adenine Dinucleotide (Fad) within 5.0Å range: probe atom residue distance (Å) B Occ C:Br807 b:39.6 occ:0.56 OG C:SER318 2.9 36.6 1.0 N C:LEU354 3.2 36.0 1.0 CA C:TYR353 3.6 37.1 1.0 O C:HOH985 3.6 48.0 1.0 CB C:SER318 3.7 32.4 1.0 CE C:MET375 3.7 31.4 1.0 CD1 C:TYR353 3.8 39.8 1.0 CB C:TYR353 3.9 37.4 1.0 C C:TYR353 3.9 36.6 1.0 CB C:LEU354 3.9 36.8 1.0 SD C:MET375 4.0 33.5 0.9 CA C:LEU354 4.2 36.7 1.0 CB C:SER348 4.3 33.2 1.0 CG C:TYR353 4.3 38.7 1.0 CG C:MET375 4.4 30.1 1.0 CE1 C:TYR353 4.8 40.5 1.0 OG C:SER348 4.9 32.3 1.0 N C:TYR353 4.9 36.7 1.0 O C:LEU354 5.0 36.4 1.0

Bromine binding site 7 out of 26 in the Spnox Dehydrogenase Domain, Mutant F397W in Complex with Flavin Adenine Dinucleotide (Fad)


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 7 of Spnox Dehydrogenase Domain, Mutant F397W in Complex with Flavin Adenine Dinucleotide (Fad) within 5.0Å range: probe atom residue distance (Å) B Occ C:Br808 b:38.9 occ:0.97 OG C:SER374 3.1 32.3 1.0 N C:SER374 3.5 29.1 1.0 CB C:SER374 3.7 30.7 1.0 N C:PHE399 3.7 47.1 1.0 CG2 C:ILE373 3.8 31.3 1.0 CB C:PRO372 3.8 29.9 1.0 N C:ILE373 3.8 27.3 1.0 CA C:LYS398 4.1 43.2 1.0 C C:PRO372 4.2 27.1 1.0 CA C:PRO372 4.2 28.2 1.0 O C:TRP397 4.2 35.0 1.0 CA C:SER374 4.3 29.6 1.0 C C:LYS398 4.4 45.8 1.0 C C:ILE373 4.5 28.8 1.0 CA C:ILE373 4.5 28.5 1.0 CB C:PHE399 4.5 49.2 1.0 CB C:ILE373 4.7 30.8 1.0 CA C:PHE399 4.7 49.0 1.0 CG C:LYS398 4.9 51.7 1.0 CB C:LYS398 4.9 46.4 1.0 O C:PHE399 4.9 52.1 1.0 N C:LYS398 5.0 39.7 1.0 C C:TRP397 5.0 36.8 1.0

Bromine binding site 8 out of 26 in the Spnox Dehydrogenase Domain, Mutant F397W in Complex with Flavin Adenine Dinucleotide (Fad)


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 8 of Spnox Dehydrogenase Domain, Mutant F397W in Complex with Flavin Adenine Dinucleotide (Fad) within 5.0Å range: probe atom residue distance (Å) B Occ C:Br809 b:35.7 occ:0.38 OG1 C:THR270 3.0 29.5 1.0 O C:HOH1092 3.1 37.7 1.0 CE C:LYS222 3.7 35.8 1.0 CB C:THR270 3.7 27.8 1.0 CG2 C:THR270 3.7 28.7 1.0 CZ C:PHE224 4.0 28.9 1.0 CD C:LYS222 4.1 31.2 1.0 O C:HOH1094 4.1 59.9 1.0 O C:HOH1009 4.2 31.2 1.0 CG C:PRO185 4.2 35.3 1.0 CE2 C:PHE224 4.3 29.4 1.0 CB C:PRO185 4.5 33.9 1.0 NZ C:LYS222 4.9 37.6 1.0

Bromine binding site 9 out of 26 in the Spnox Dehydrogenase Domain, Mutant F397W in Complex with Flavin Adenine Dinucleotide (Fad)


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 9 of Spnox Dehydrogenase Domain, Mutant F397W in Complex with Flavin Adenine Dinucleotide (Fad) within 5.0Å range: probe atom residue distance (Å) B Occ F:Br802 b:41.3 occ:0.65 NH2 F:ARG209 3.2 36.0 1.0 N F:PHE184 3.4 33.4 1.0 NE2 C:HIS364 3.4 38.9 1.0 CE1 C:HIS364 3.5 38.5 1.0 CA F:SER183 3.7 38.8 1.0 O C:HOH1040 3.7 44.1 1.0 O F:PHE184 4.0 30.9 1.0 CB F:SER183 4.0 40.7 1.0 C F:SER183 4.0 35.6 1.0 CZ F:ARG209 4.1 36.1 1.0 CG C:PRO362A 4.1 41.2 1.0 O F:HOH985 4.3 41.4 1.0 O F:ILE182 4.3 44.3 1.0 CA F:PHE184 4.4 31.7 1.0 NE F:ARG209 4.4 34.0 1.0 CB F:PHE184 4.5 30.5 1.0 CB C:PRO362A 4.5 40.8 1.0 CD1 F:PHE184 4.5 30.0 1.0 C F:PHE184 4.6 31.3 1.0 CD2 C:HIS364 4.7 38.0 1.0 ND1 C:HIS364 4.8 37.9 1.0 N F:SER183 4.9 40.2 1.0 O F:HOH901 4.9 48.4 1.0 CD C:PRO362A 5.0 40.1 1.0

Bromine binding site 10 out of 26 in the Spnox Dehydrogenase Domain, Mutant F397W in Complex with Flavin Adenine Dinucleotide (Fad)


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 10 of Spnox Dehydrogenase Domain, Mutant F397W in Complex with Flavin Adenine Dinucleotide (Fad) within 5.0Å range: probe atom residue distance (Å) B Occ F:Br803 b:35.1 occ:0.37 O F:HOH1016 2.9 44.7 1.0 O F:HOH1073 2.9 56.8 1.0 N F:LEU330 3.3 31.4 1.0 CA F:TYR327 3.5 26.0 1.0 C F:TYR327 3.7 27.2 1.0 N F:ASP329 3.7 31.3 1.0 CB F:ASP329 3.7 37.2 1.0 CB F:LEU330 3.8 31.4 1.0 O F:TYR327 4.0 27.1 1.0 CA F:ASP329 4.0 33.2 1.0 C F:ASP329 4.1 32.8 1.0 CA F:LEU330 4.1 30.8 1.0 N F:LEU328 4.1 27.9 1.0 O F:HOH1058 4.2 68.7 1.0 O F:HOH1026 4.3 29.7 1.0 N F:TYR327 4.4 24.5 1.0 CD1 F:TYR327 4.4 26.3 1.0 O F:HOH1098 4.4 65.0 1.0 CB F:TYR327 4.5 25.6 1.0 C F:LEU328 4.6 31.3 1.0 CG F:ASP329 4.7 46.2 1.0 OD2 F:ASP329 4.8 50.0 1.0 CG F:TYR327 4.9 25.7 1.0 CG F:LEU330 5.0 33.8 1.0 CD1 F:LEU330 5.0 33.9 1.0 O F:HOH1031 5.0 29.7 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