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Chlorine in PDB 3m0o: Crystal Structure of the LYS265MET Mutant of Monomeric Sarcosine Oxidase

Enzymatic activity of Crystal Structure of the LYS265MET Mutant of Monomeric Sarcosine Oxidase

All present enzymatic activity of Crystal Structure of the LYS265MET Mutant of Monomeric Sarcosine Oxidase:
1.5.3.1;

Protein crystallography data

The structure of Crystal Structure of the LYS265MET Mutant of Monomeric Sarcosine Oxidase, PDB code: 3m0o was solved by F.S.Mathews, Z.-W.Chen, M.S.Jorns, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.12 / 1.60
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 72.565, 69.617, 73.978, 90.00, 93.91, 90.00
R / Rfree (%) 17.3 / 20.8

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of the LYS265MET Mutant of Monomeric Sarcosine Oxidase (pdb code 3m0o). 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 the LYS265MET Mutant of Monomeric Sarcosine Oxidase, PDB code: 3m0o:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 3m0o

Go back to Chlorine Binding Sites List in 3m0o
Chlorine binding site 1 out of 2 in the Crystal Structure of the LYS265MET Mutant of Monomeric Sarcosine Oxidase


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 LYS265MET Mutant of Monomeric Sarcosine Oxidase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl405

b:15.4
occ:1.00
O A:HOH444 3.0 14.5 1.0
O3' A:FAD400 3.0 11.8 1.0
N A:GLY344 3.2 12.8 1.0
N A:THR318 3.3 15.1 1.0
C3' A:FAD400 3.5 11.1 1.0
N A:SER343 3.5 13.2 1.0
CA A:TYR317 3.6 14.8 1.0
C A:PHE342 3.7 13.9 1.0
CA A:GLY344 3.8 12.4 1.0
C A:TYR317 3.9 15.3 1.0
CB A:PHE342 4.0 14.0 1.0
O A:HOH398 4.0 13.8 1.0
CA A:PHE342 4.2 13.3 1.0
C5' A:FAD400 4.2 11.6 1.0
C A:SER343 4.2 14.1 1.0
O A:MET316 4.2 14.3 1.0
CB A:TYR317 4.2 14.6 1.0
O A:PHE342 4.2 13.5 1.0
CA A:SER343 4.3 13.9 1.0
O A:THR318 4.3 14.7 1.0
N A:PHE342 4.3 13.7 1.0
C1' A:FAD400 4.4 12.5 1.0
CA A:THR318 4.4 14.6 1.0
C4' A:FAD400 4.5 9.5 1.0
C2' A:FAD400 4.6 10.8 1.0
CB A:THR318 4.6 14.3 1.0
CD1 A:TYR317 4.7 12.1 1.0
OG A:SER43 4.7 12.4 1.0
C A:THR318 4.7 15.0 1.0
N A:TYR317 4.7 13.6 1.0
C A:GLY344 4.7 13.0 1.0
OG1 A:THR318 4.7 14.9 1.0
CG A:TYR317 4.8 13.9 1.0
CB A:SER43 4.8 13.5 1.0
N A:HIS345 4.8 12.9 1.0
C A:MET316 4.9 14.0 1.0

Chlorine binding site 2 out of 2 in 3m0o

Go back to Chlorine Binding Sites List in 3m0o
Chlorine binding site 2 out of 2 in the Crystal Structure of the LYS265MET Mutant of Monomeric Sarcosine Oxidase


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 LYS265MET Mutant of Monomeric Sarcosine Oxidase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl406

b:15.3
occ:1.00
O B:HOH395 2.9 15.4 1.0
O3' B:FAD400 3.1 14.5 1.0
N B:GLY344 3.2 12.9 1.0
N B:THR318 3.3 14.8 1.0
N B:SER343 3.5 13.9 1.0
C3' B:FAD400 3.5 12.3 1.0
CA B:TYR317 3.6 14.4 1.0
C B:PHE342 3.7 14.1 1.0
CA B:GLY344 3.8 13.2 1.0
C B:TYR317 3.9 15.2 1.0
CB B:PHE342 4.0 14.2 1.0
O B:HOH411 4.0 14.9 1.0
CA B:PHE342 4.1 13.5 1.0
O B:MET316 4.2 13.9 1.0
C5' B:FAD400 4.2 13.5 1.0
C B:SER343 4.2 14.0 1.0
CB B:TYR317 4.2 14.3 1.0
CA B:SER343 4.3 13.6 1.0
O B:PHE342 4.3 14.5 1.0
O B:THR318 4.3 14.2 1.0
N B:PHE342 4.3 14.4 1.0
CA B:THR318 4.4 14.7 1.0
C1' B:FAD400 4.4 13.6 1.0
C4' B:FAD400 4.5 11.6 1.0
CB B:THR318 4.6 15.0 1.0
OG B:SER43 4.6 14.7 1.0
CD1 B:TYR317 4.6 14.9 1.0
OG1 B:THR318 4.7 17.5 1.0
C2' B:FAD400 4.7 13.9 1.0
N B:TYR317 4.7 13.9 1.0
C B:THR318 4.7 14.7 1.0
CG B:TYR317 4.8 14.7 1.0
C B:GLY344 4.8 13.4 1.0
CB B:SER43 4.8 15.2 1.0
C B:MET316 4.9 14.2 1.0
N B:HIS345 4.9 12.9 1.0

Reference:

M.S.Jorns, Z.W.Chen, F.S.Mathews. Structural Characterization of Mutations at the Oxygen Activation Site in Monomeric Sarcosine Oxidase . Biochemistry V. 49 3631 2010.
ISSN: ISSN 0006-2960
PubMed: 20353187
DOI: 10.1021/BI100160J
Page generated: Fri Jul 11 07:42:02 2025

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