Chlorine in PDB 3bhk: Crystal Structure of R49K Mutant of Monomeric Sarcosine Oxidase Crystallized in Phosphate As Precipitant

All present enzymatic activity of Crystal Structure of R49K Mutant of Monomeric Sarcosine Oxidase Crystallized in Phosphate As Precipitant:
1.5.3.1;

The structure of Crystal Structure of R49K Mutant of Monomeric Sarcosine Oxidase Crystallized in Phosphate As Precipitant, PDB code: 3bhk was solved by A.Hassan-Abdallah, G.Zhao, Z.Chen, F.S.Mathews, M.S.Jorns, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	32.40 / 1.71
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	72.653, 69.655, 73.357, 90.00, 93.74, 90.00
R / Rfree (%)	17.2 / 20.8

The binding sites of Chlorine atom in the Crystal Structure of R49K Mutant of Monomeric Sarcosine Oxidase Crystallized in Phosphate As Precipitant (pdb code 3bhk). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of R49K Mutant of Monomeric Sarcosine Oxidase Crystallized in Phosphate As Precipitant, PDB code: 3bhk:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of R49K Mutant of Monomeric Sarcosine Oxidase Crystallized in Phosphate As Precipitant


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 R49K Mutant of Monomeric Sarcosine Oxidase Crystallized in Phosphate As Precipitant within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl401 b:16.0 occ:1.00 O3' A:FAD400 3.0 14.8 1.0 O A:HOH923 3.0 17.3 1.0 N A:GLY344 3.2 15.5 1.0 N A:THR318 3.4 17.4 1.0 C3' A:FAD400 3.4 14.4 1.0 CA A:TYR317 3.6 15.9 1.0 N A:SER343 3.7 15.2 1.0 C A:PHE342 3.8 14.9 1.0 CA A:GLY344 3.9 15.3 1.0 CB A:PHE342 3.9 13.6 1.0 C A:TYR317 4.0 18.1 1.0 O A:HOH933 4.0 16.0 1.0 CA A:PHE342 4.1 14.4 1.0 C A:SER343 4.1 16.4 1.0 O A:MET316 4.2 15.3 1.0 CA A:SER343 4.2 15.6 1.0 C5' A:FAD400 4.2 14.4 1.0 O A:PHE342 4.2 15.1 1.0 O A:THR318 4.3 17.3 1.0 N A:PHE342 4.3 13.6 1.0 C1' A:FAD400 4.3 14.4 1.0 CB A:TYR317 4.3 16.4 1.0 CA A:THR318 4.4 18.2 1.0 CB A:THR318 4.6 19.2 1.0 OG A:SER43 4.6 17.8 1.0 C4' A:FAD400 4.6 14.9 1.0 C2' A:FAD400 4.6 13.9 1.0 C A:THR318 4.7 18.8 1.0 OG1 A:THR318 4.7 19.8 1.0 CD1 A:TYR317 4.7 16.2 1.0 N A:TYR317 4.7 14.3 1.0 C A:GLY344 4.8 14.2 1.0 CG A:TYR317 4.9 16.2 1.0 CB A:SER43 4.9 14.7 1.0 N A:HIS345 4.9 13.8 1.0 C A:MET316 4.9 16.0 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of R49K Mutant of Monomeric Sarcosine Oxidase Crystallized in Phosphate As Precipitant


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 R49K Mutant of Monomeric Sarcosine Oxidase Crystallized in Phosphate As Precipitant within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl401 b:16.4 occ:1.00 O B:HOH1127 3.0 16.1 1.0 O3' B:FAD400 3.0 14.0 1.0 N B:GLY344 3.1 14.3 1.0 N B:THR318 3.3 15.3 1.0 C3' B:FAD400 3.5 13.8 1.0 CA B:TYR317 3.6 15.0 1.0 N B:SER343 3.6 14.3 1.0 C B:PHE342 3.7 14.0 1.0 C B:TYR317 3.9 15.9 1.0 CA B:GLY344 3.9 13.3 1.0 CB B:PHE342 3.9 12.5 1.0 O B:HOH1121 4.0 16.2 1.0 CA B:PHE342 4.1 12.7 1.0 C B:SER343 4.1 15.5 1.0 O B:MET316 4.2 13.1 1.0 O B:PHE342 4.2 14.1 1.0 CA B:SER343 4.2 15.2 1.0 C5' B:FAD400 4.2 12.7 1.0 O B:THR318 4.3 12.5 1.0 CB B:TYR317 4.3 12.4 1.0 C1' B:FAD400 4.3 13.4 1.0 CA B:THR318 4.3 15.5 1.0 N B:PHE342 4.3 13.0 1.0 CB B:THR318 4.5 14.3 1.0 OG B:SER43 4.6 15.9 1.0 C4' B:FAD400 4.6 13.6 1.0 C2' B:FAD400 4.6 15.2 1.0 OG1 B:THR318 4.7 19.1 1.0 C B:THR318 4.7 14.1 1.0 CD1 B:TYR317 4.7 11.6 1.0 N B:TYR317 4.7 14.9 1.0 C B:GLY344 4.8 15.2 1.0 CG B:TYR317 4.9 12.7 1.0 C B:MET316 4.9 14.1 1.0 N B:HIS345 4.9 13.9 1.0 CB B:SER43 4.9 14.1 1.0

A.Hassan-Abdallah, G.Zhao, Z.W.Chen, F.S.Mathews, M.Schuman Jorns. Arginine 49 Is A Bifunctional Residue Important in Catalysis and Biosynthesis of Monomeric Sarcosine Oxidase: A Context-Sensitive Model For the Electrostatic Impact of Arginine to Lysine Mutations. Biochemistry V. 47 2913 2008.
ISSN: ISSN 0006-2960
PubMed: 18251505
DOI: 10.1021/BI702351V