Chlorine in PDB 1ahz: Structure of the Octameric Flavoenzyme Vanillyl-Alcohol Oxidase in Complex with 4-(1-Heptenyl)Phenol

All present enzymatic activity of Structure of the Octameric Flavoenzyme Vanillyl-Alcohol Oxidase in Complex with 4-(1-Heptenyl)Phenol:
1.1.3.13;

The structure of Structure of the Octameric Flavoenzyme Vanillyl-Alcohol Oxidase in Complex with 4-(1-Heptenyl)Phenol, PDB code: 1ahz was solved by A.Mattevi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 3.30
Space group	I 4
Cell size a, b, c (Å), α, β, γ (°)	140.970, 140.970, 133.450, 90.00, 90.00, 90.00
R / Rfree (%)	22.4 / 26.8

The binding sites of Chlorine atom in the Structure of the Octameric Flavoenzyme Vanillyl-Alcohol Oxidase in Complex with 4-(1-Heptenyl)Phenol (pdb code 1ahz). 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 the Octameric Flavoenzyme Vanillyl-Alcohol Oxidase in Complex with 4-(1-Heptenyl)Phenol, PDB code: 1ahz:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Structure of the Octameric Flavoenzyme Vanillyl-Alcohol Oxidase in Complex with 4-(1-Heptenyl)Phenol


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of the Octameric Flavoenzyme Vanillyl-Alcohol Oxidase in Complex with 4-(1-Heptenyl)Phenol within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl601 b:34.0 occ:1.00 O A:LEU171 3.1 50.0 1.0 O2' A:FAD600 3.2 23.1 1.0 C10 A:FAD600 3.4 14.4 1.0 C4X A:FAD600 3.5 12.9 1.0 CB A:LEU171 3.5 32.9 1.0 N10 A:FAD600 3.5 13.4 1.0 N5 A:FAD600 3.5 13.0 1.0 C9A A:FAD600 3.5 11.8 1.0 C5X A:FAD600 3.6 14.0 1.0 N A:LEU171 3.6 29.6 1.0 C3' A:FAD600 3.7 17.8 1.0 C A:LEU171 3.9 40.0 1.0 C2' A:FAD600 3.9 17.8 1.0 CA A:LEU171 3.9 33.3 1.0 OH A:TYR51 3.9 52.3 1.0 CG A:LEU171 3.9 33.1 1.0 CD1 A:LEU171 4.1 29.9 1.0 N1 A:FAD600 4.2 15.2 1.0 C9 A:FAD600 4.2 10.7 1.0 C1' A:FAD600 4.3 14.3 1.0 C4 A:FAD600 4.3 14.8 1.0 CB A:PRO169 4.3 12.4 1.0 C6 A:FAD600 4.3 11.6 1.0 C4' A:FAD600 4.4 12.0 1.0 N A:ASP170 4.5 24.1 1.0 CG A:PRO169 4.5 22.9 1.0 C A:ASP170 4.5 39.6 1.0 O4' A:FAD600 4.8 8.8 1.0 C2 A:FAD600 4.8 18.0 1.0 O3' A:FAD600 4.8 21.4 1.0 CA A:ASP170 4.8 24.9 1.0 C8 A:FAD600 4.9 9.8 1.0 N3 A:FAD600 4.9 17.0 1.0 C7 A:FAD600 4.9 9.0 1.0 O4 A:FAD600 4.9 14.1 1.0 CZ A:TYR51 4.9 48.5 1.0

Chlorine binding site 2 out of 2 in the Structure of the Octameric Flavoenzyme Vanillyl-Alcohol Oxidase in Complex with 4-(1-Heptenyl)Phenol


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Structure of the Octameric Flavoenzyme Vanillyl-Alcohol Oxidase in Complex with 4-(1-Heptenyl)Phenol within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl601 b:34.0 occ:1.00 O B:LEU171 3.1 50.0 1.0 O2' B:FAD600 3.2 23.1 1.0 C10 B:FAD600 3.4 14.4 1.0 C4X B:FAD600 3.5 12.9 1.0 CB B:LEU171 3.5 32.9 1.0 N10 B:FAD600 3.5 13.4 1.0 N5 B:FAD600 3.5 13.0 1.0 C9A B:FAD600 3.5 11.8 1.0 C5X B:FAD600 3.6 14.0 1.0 N B:LEU171 3.6 29.6 1.0 C3' B:FAD600 3.7 17.8 1.0 C B:LEU171 3.9 40.0 1.0 C2' B:FAD600 3.9 17.8 1.0 CA B:LEU171 3.9 33.3 1.0 OH B:TYR51 3.9 52.3 1.0 CG B:LEU171 3.9 33.1 1.0 CD1 B:LEU171 4.1 29.9 1.0 N1 B:FAD600 4.2 15.2 1.0 C9 B:FAD600 4.2 10.7 1.0 C1' B:FAD600 4.3 14.3 1.0 C4 B:FAD600 4.3 14.8 1.0 CB B:PRO169 4.3 12.4 1.0 C6 B:FAD600 4.3 11.6 1.0 C4' B:FAD600 4.4 12.0 1.0 N B:ASP170 4.5 24.1 1.0 CG B:PRO169 4.5 22.9 1.0 C B:ASP170 4.5 39.6 1.0 O4' B:FAD600 4.8 8.8 1.0 C2 B:FAD600 4.8 18.0 1.0 O3' B:FAD600 4.8 21.4 1.0 CA B:ASP170 4.8 24.9 1.0 C8 B:FAD600 4.9 9.8 1.0 N3 B:FAD600 4.9 17.0 1.0 C7 B:FAD600 4.9 9.0 1.0 O4 B:FAD600 4.9 14.1 1.0 CZ B:TYR51 4.9 48.5 1.0

A.Mattevi, M.W.Fraaije, A.Mozzarelli, L.Olivi, A.Coda, W.J.Van Berkel. Crystal Structures and Inhibitor Binding in the Octameric Flavoenzyme Vanillyl-Alcohol Oxidase: the Shape of the Active-Site Cavity Controls Substrate Specificity. Structure V. 5 907 1997.
ISSN: ISSN 0969-2126
PubMed: 9261083
DOI: 10.1016/S0969-2126(97)00245-1