Chlorine in PDB 9f1o: Crystal Structure of the Dyp-Type Peroxidase Pross Variant From Pseudomonas Putida

The structure of Crystal Structure of the Dyp-Type Peroxidase Pross Variant From Pseudomonas Putida, PDB code: 9f1o was solved by L.Constanca, P.T.Borges, C.Frazao, L.O.Martins, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	70.75 / 2.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	49.974, 84.812, 128.276, 90, 90, 90
R / Rfree (%)	19.4 / 22.9

The structure of Crystal Structure of the Dyp-Type Peroxidase Pross Variant From Pseudomonas Putida also contains other interesting chemical elements:

Iron

(Fe)

2 atoms

The binding sites of Chlorine atom in the Crystal Structure of the Dyp-Type Peroxidase Pross Variant From Pseudomonas Putida (pdb code 9f1o). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Crystal Structure of the Dyp-Type Peroxidase Pross Variant From Pseudomonas Putida, PDB code: 9f1o:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the Crystal Structure of the Dyp-Type Peroxidase Pross Variant From Pseudomonas Putida


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 the Dyp-Type Peroxidase Pross Variant From Pseudomonas Putida within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl303 b:56.8 occ:1.00 CG A:PRO30 3.8 53.5 1.0 CD2 A:LEU29 4.0 47.2 1.0 CG A:LEU29 4.1 46.7 1.0 CD A:PRO30 4.2 52.3 1.0 CD2 A:LEU285 4.2 45.2 1.0 N A:PRO30 4.3 49.1 1.0 CA A:PRO30 4.3 50.4 1.0 CD1 A:LEU33 4.4 42.2 1.0 CB A:PRO30 4.4 52.2 1.0 CD2 A:LEU57 4.5 42.9 1.0 CB A:LEU29 4.6 44.1 1.0 C A:LEU29 4.8 43.9 1.0

Chlorine binding site 2 out of 4 in the Crystal Structure of the Dyp-Type Peroxidase Pross Variant From Pseudomonas Putida


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 the Dyp-Type Peroxidase Pross Variant From Pseudomonas Putida within 5.0Å range:

Chlorine binding site 3 out of 4 in the Crystal Structure of the Dyp-Type Peroxidase Pross Variant From Pseudomonas Putida


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 the Dyp-Type Peroxidase Pross Variant From Pseudomonas Putida within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl303 b:58.1 occ:1.00 O B:LYS161 3.5 40.9 1.0 NE2 A:GLN24 3.5 63.7 1.0 O B:HOH429 3.8 45.8 1.0 O B:PHE260 4.1 44.6 1.0 NE B:ARG262 4.1 48.3 1.0 N B:ASP163 4.2 50.8 1.0 CG B:LYS161 4.2 36.8 1.0 CB B:ASP163 4.2 56.0 1.0 C B:HIS162 4.3 48.0 1.0 C B:LYS161 4.3 37.7 1.0 CE B:LYS161 4.3 50.3 1.0 CG B:ARG262 4.3 45.3 1.0 CD B:LYS161 4.4 40.7 1.0 CD B:ARG262 4.5 47.7 1.0 CD A:GLN24 4.5 60.2 1.0 CA B:HIS162 4.6 44.0 1.0 O B:HIS162 4.6 45.7 1.0 C B:PHE260 4.7 41.9 1.0 CA B:SER261 4.7 33.7 1.0 N B:HIS162 4.7 36.5 1.0 OE1 A:GLN24 4.8 61.5 1.0 CA B:ASP163 4.8 53.8 1.0 N B:ARG262 4.8 36.2 1.0 CB B:LYS161 4.8 31.7 1.0 N B:SER261 4.9 35.9 1.0

Chlorine binding site 4 out of 4 in the Crystal Structure of the Dyp-Type Peroxidase Pross Variant From Pseudomonas Putida


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 the Dyp-Type Peroxidase Pross Variant From Pseudomonas Putida within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl304 b:61.7 occ:1.00 N B:SER195 3.7 48.9 1.0 OG B:SER195 3.8 47.3 1.0 CB B:PRO193 3.8 51.2 1.0 N B:GLU194 3.9 48.1 1.0 CG2 B:ILE253 3.9 39.8 1.0 CB B:SER195 3.9 43.7 1.0 CD1 B:ILE253 4.2 46.9 1.0 CB B:GLU194 4.4 46.9 1.0 CA B:SER195 4.4 42.6 1.0 CA B:GLU194 4.4 46.4 1.0 C B:GLU194 4.5 43.1 1.0 C B:PRO193 4.5 49.0 1.0 CA B:PRO193 4.5 54.6 1.0 CG1 B:ILE253 4.8 47.2 1.0 CG B:PRO193 5.0 51.7 1.0

D.Silva, C.F.Rodrigues, C.Lorena, C.Frazao, P.T.Borges, L.O.Martins. One-Step Computational Design of Hyperthermostable Bacterial Dyp-Type Peroxidases To Be Published.