Chlorine in PDB 2ifv: Crystal Structure of An Active Site Mutant, C473D, of CDC25B Phosphatase Catalytic Domain

All present enzymatic activity of Crystal Structure of An Active Site Mutant, C473D, of CDC25B Phosphatase Catalytic Domain:
3.1.3.48;

The structure of Crystal Structure of An Active Site Mutant, C473D, of CDC25B Phosphatase Catalytic Domain, PDB code: 2ifv was solved by J.Rudolph, G.Buhrman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.69 / 1.60
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	49.895, 71.189, 73.870, 90.00, 90.00, 90.00
R / Rfree (%)	17.9 / 19.2

The binding sites of Chlorine atom in the Crystal Structure of An Active Site Mutant, C473D, of CDC25B Phosphatase Catalytic Domain (pdb code 2ifv). 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 An Active Site Mutant, C473D, of CDC25B Phosphatase Catalytic Domain, PDB code: 2ifv:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of An Active Site Mutant, C473D, of CDC25B Phosphatase Catalytic Domain


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 An Active Site Mutant, C473D, of CDC25B Phosphatase Catalytic Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl551 b:12.6 occ:1.00 O A:HOH665 3.0 29.7 1.0 O A:HOH559 3.1 10.8 1.0 N A:ARG548 3.3 11.9 1.0 N A:GLU446 3.3 10.3 1.0 O A:HOH671 3.3 26.7 1.0 CA A:THR547 3.8 11.2 1.0 CG A:GLU446 3.9 15.1 1.0 CA A:LEU445 3.9 9.1 1.0 CB A:ARG548 3.9 17.2 1.0 CD2 A:LEU445 3.9 11.8 1.0 CB A:THR547 3.9 11.8 1.0 CB A:GLU446 3.9 12.2 1.0 C A:THR547 4.0 11.9 1.0 C A:LEU445 4.1 9.6 1.0 CA A:ARG548 4.2 14.1 1.0 CA A:GLU446 4.2 10.9 1.0 CB A:LEU445 4.3 9.6 1.0 NH1 A:ARG447 4.3 10.7 1.0 CG2 A:THR547 4.4 13.0 1.0 CD A:GLU446 4.5 17.1 1.0 OE1 A:GLU446 4.7 21.8 1.0 O A:PRO444 4.7 11.2 1.0 CG A:LEU445 4.8 9.9 1.0 O A:HOH765 4.9 45.0 1.0 O A:HOH692 4.9 26.1 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of An Active Site Mutant, C473D, of CDC25B Phosphatase Catalytic Domain


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 An Active Site Mutant, C473D, of CDC25B Phosphatase Catalytic Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl552 b:25.8 occ:1.00 OG A:SER476 3.1 22.8 1.0 N A:LYS394 3.1 20.0 1.0 O A:SER476 3.4 30.0 1.0 O A:HOH633 3.6 24.3 1.0 CB A:LYS394 3.6 23.3 1.0 CE A:LYS509 3.6 21.4 1.0 CD A:LYS509 3.7 18.3 1.0 CE2 A:TYR400 3.8 12.0 1.0 O A:HOH790 3.8 41.2 1.0 CA A:GLY393 3.9 19.7 1.0 CA A:LYS394 3.9 21.7 1.0 C A:GLY393 3.9 19.7 1.0 CB A:SER476 4.1 29.1 1.0 CZ A:TYR400 4.3 14.1 1.0 OH A:TYR400 4.3 16.0 1.0 CD2 A:TYR400 4.4 10.8 1.0 C A:SER476 4.5 28.8 1.0 O A:HOH771 4.8 39.8 1.0 O A:HOH760 4.8 39.3 1.0 NZ A:LYS509 4.9 25.4 1.0 CA A:SER476 4.9 27.8 1.0 CG A:LYS394 5.0 28.7 1.0

J.Sohn, G.Buhrman, J.Rudolph. Kinetic and Structural Studies of Specific Protein-Protein Interactions in Substrate Catalysis By CDC25B Phosphatase. Biochemistry V. 46 807 2007.
ISSN: ISSN 0006-2960
PubMed: 17223702
DOI: 10.1021/BI061257Y