Chlorine in PDB 8s7w: Vanillyl-Alcohol Dehydrogenase From Marinicaulis Flavus: P151V Mutant

The structure of Vanillyl-Alcohol Dehydrogenase From Marinicaulis Flavus: P151V Mutant, PDB code: 8s7w was solved by T.B.Guerriere, A.Mattevi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.86 / 2.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	100.621, 114.641, 130.709, 90, 90, 90
R / Rfree (%)	17.2 / 20.9

The binding sites of Chlorine atom in the Vanillyl-Alcohol Dehydrogenase From Marinicaulis Flavus: P151V Mutant (pdb code 8s7w). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 5 binding sites of Chlorine where determined in the Vanillyl-Alcohol Dehydrogenase From Marinicaulis Flavus: P151V Mutant, PDB code: 8s7w:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5;

Chlorine binding site 1 out of 5 in the Vanillyl-Alcohol Dehydrogenase From Marinicaulis Flavus: P151V Mutant


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Vanillyl-Alcohol Dehydrogenase From Marinicaulis Flavus: P151V Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl602 b:10.3 occ:1.00 O A:HOH958 3.1 34.6 1.0 N A:GLY515 3.1 26.9 1.0 CB A:PRO508 3.6 22.4 1.0 O A:GLY504 3.8 27.1 1.0 CA A:PRO508 3.8 20.6 1.0 CG A:PRO508 3.9 22.4 1.0 CA A:GLY504 3.9 22.8 1.0 CA A:GLY515 4.0 26.9 1.0 C A:TRP514 4.0 25.2 1.0 CA A:TRP514 4.0 23.1 1.0 CE A:LYS497 4.0 20.6 1.0 C A:GLY504 4.2 24.6 1.0 CD A:ARG518 4.4 31.6 1.0 N A:PRO508 4.5 21.4 1.0 CG A:ARG518 4.6 27.6 1.0 NZ A:LYS497 4.6 19.1 1.0 CD A:PRO508 4.7 22.4 1.0 CB A:ARG518 4.7 28.9 1.0 O A:LEU506 4.7 16.8 1.0 CE3 A:TRP514 4.7 21.9 1.0 CB A:TRP514 4.8 21.5 1.0 C A:GLY515 4.8 25.6 1.0 O A:ILE513 4.9 19.8 1.0 O A:GLY515 4.9 20.6 1.0 NE A:ARG518 4.9 31.7 1.0 C A:PRO508 5.0 20.6 1.0

Chlorine binding site 2 out of 5 in the Vanillyl-Alcohol Dehydrogenase From Marinicaulis Flavus: P151V Mutant


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Vanillyl-Alcohol Dehydrogenase From Marinicaulis Flavus: P151V Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl603 b:34.1 occ:1.00 NH2 A:ARG191 4.0 25.9 1.0 CE A:LYS228 4.1 20.8 1.0 CD2 A:LEU123 4.1 19.5 1.0 CD A:LYS228 4.3 21.9 1.0 CD1 A:LEU113 4.3 24.5 1.0 NH1 A:ARG191 4.5 29.5 1.0 CZ3 A:TRP203 4.6 19.3 1.0 CZ A:ARG191 4.7 27.2 1.0

Chlorine binding site 3 out of 5 in the Vanillyl-Alcohol Dehydrogenase From Marinicaulis Flavus: P151V Mutant


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Vanillyl-Alcohol Dehydrogenase From Marinicaulis Flavus: P151V Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl607 b:30.0 occ:1.00 N B:ALA238 3.8 28.5 1.0 CA B:PRO237 4.1 25.1 1.0 O A:HOH703 4.1 43.0 1.0 O B:HOH794 4.1 28.2 1.0 CA B:GLY323 4.3 30.0 1.0 CB B:ALA238 4.3 31.1 1.0 CD B:PRO324 4.3 34.9 1.0 CB B:PRO237 4.4 27.9 1.0 C B:PRO237 4.5 26.4 1.0 C1 A:PEG606 4.5 56.6 1.0 O1 A:PEG606 4.7 57.3 1.0 CA B:ALA238 4.7 31.2 1.0 CB A:ALA266 5.0 23.8 1.0 N B:PRO324 5.0 36.7 1.0

Chlorine binding site 4 out of 5 in the Vanillyl-Alcohol Dehydrogenase From Marinicaulis Flavus: P151V Mutant


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Vanillyl-Alcohol Dehydrogenase From Marinicaulis Flavus: P151V Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl608 b:40.0 occ:1.00 CE B:LYS228 4.0 21.1 1.0 NH2 B:ARG191 4.1 26.7 1.0 CD B:LYS228 4.2 20.2 1.0 CD2 B:LEU123 4.2 18.7 1.0 CD1 B:LEU113 4.3 26.4 1.0 NH1 B:ARG191 4.7 27.2 1.0 CZ3 B:TRP203 4.8 19.3 1.0 CZ B:ARG191 4.8 26.2 1.0 CD2 B:LEU113 4.8 26.1 1.0 CG B:LEU113 4.9 26.5 1.0 CB B:LEU113 5.0 23.0 1.0

Chlorine binding site 5 out of 5 in the Vanillyl-Alcohol Dehydrogenase From Marinicaulis Flavus: P151V Mutant


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 5 of Vanillyl-Alcohol Dehydrogenase From Marinicaulis Flavus: P151V Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl609 b:17.2 occ:1.00 N B:GLY515 3.1 31.7 1.0 CB B:PRO508 3.5 26.0 1.0 O B:GLY504 3.7 33.0 1.0 CA B:PRO508 3.7 23.4 1.0 CA B:GLY504 3.8 25.4 1.0 CA B:GLY515 3.9 31.6 1.0 CG B:PRO508 4.0 26.4 1.0 O B:HOH701 4.0 38.0 1.0 CA B:TRP514 4.0 30.6 1.0 C B:TRP514 4.0 33.3 1.0 CE B:LYS497 4.0 19.9 1.0 C B:GLY504 4.1 28.2 1.0 CD B:ARG518 4.5 37.6 1.0 N B:PRO508 4.5 23.7 1.0 CG B:ARG518 4.6 36.0 1.0 NZ B:LYS497 4.6 20.6 1.0 O B:LEU506 4.7 22.4 1.0 CB B:TRP514 4.8 28.9 1.0 CB B:ARG518 4.8 36.8 1.0 C B:GLY515 4.8 31.1 1.0 O B:ILE513 4.8 23.6 1.0 CD B:PRO508 4.9 24.7 1.0 O B:GLY515 4.9 27.4 1.0 C B:PRO508 4.9 24.1 1.0 CE3 B:TRP514 4.9 25.6 1.0

T.B.Guerriere, A.Vancheri, I.Ricotti, S.A.Serapian, D.Eggerichs, D.Tischler, G.Colombo, M.L.Mascotti, M.W.Fraaije, A.Mattevi. Dehydrogenase Versus Oxidase Function: the Interplay Between Substrate Binding and Flavin Microenvironment Acs Catalysis 1046 2025.
ISSN: ESSN 2155-5435
DOI: 10.1021/ACSCATAL.4C05944