Chlorine in PDB 2ifd: Crystal Structure of A Remote Binding Site Mutant, R492L, of CDC25B Phosphatase Catalytic Domain

All present enzymatic activity of Crystal Structure of A Remote Binding Site Mutant, R492L, of CDC25B Phosphatase Catalytic Domain:
3.1.3.48;

The structure of Crystal Structure of A Remote Binding Site Mutant, R492L, of CDC25B Phosphatase Catalytic Domain, PDB code: 2ifd 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)	29.03 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	49.957, 71.320, 75.060, 90.00, 90.00, 90.00
R / Rfree (%)	19.1 / 21.2

The binding sites of Chlorine atom in the Crystal Structure of A Remote Binding Site Mutant, R492L, of CDC25B Phosphatase Catalytic Domain (pdb code 2ifd). 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 A Remote Binding Site Mutant, R492L, of CDC25B Phosphatase Catalytic Domain, PDB code: 2ifd:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of A Remote Binding Site Mutant, R492L, 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 A Remote Binding Site Mutant, R492L, of CDC25B Phosphatase Catalytic Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl201 b:20.5 occ:1.00 O A:HOH65 2.9 21.6 1.0 O A:HOH13 3.0 14.1 1.0 N A:GLU446 3.3 14.3 1.0 N A:ARG548 3.4 17.8 1.0 CG A:GLU446 3.8 22.5 1.0 CA A:THR547 3.8 15.9 1.0 CA A:LEU445 3.9 12.6 1.0 CG A:ARG548 3.9 32.7 1.0 CB A:THR547 4.0 16.3 1.0 CD2 A:LEU445 4.0 13.1 1.0 CB A:GLU446 4.0 18.9 1.0 CD A:ARG548 4.0 37.0 1.0 C A:LEU445 4.1 14.1 1.0 CB A:ARG548 4.1 24.9 1.0 C A:THR547 4.2 16.7 1.0 CA A:GLU446 4.2 16.1 1.0 NH1 A:ARG447 4.3 13.6 1.0 CB A:LEU445 4.3 13.0 1.0 CG2 A:THR547 4.3 16.6 1.0 CA A:ARG548 4.4 20.9 1.0 CD A:GLU446 4.6 27.1 1.0 O A:PRO444 4.8 14.1 1.0 CG A:LEU445 4.8 13.4 1.0 OE1 A:GLU446 4.8 27.2 1.0 N A:ARG447 4.9 15.9 1.0 NE A:ARG548 5.0 38.1 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of A Remote Binding Site Mutant, R492L, 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 A Remote Binding Site Mutant, R492L, of CDC25B Phosphatase Catalytic Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl202 b:44.0 occ:1.00 CE A:LYS509 3.4 27.6 1.0 O A:HOH23 3.4 17.0 1.0 N A:LYS394 3.5 23.0 1.0 O A:HOH36 3.8 15.7 1.0 CD A:LYS509 3.9 24.2 1.0 CB A:LYS394 3.9 26.4 1.0 CA A:GLY393 4.2 21.0 1.0 CA A:LYS394 4.3 24.9 1.0 C A:GLY393 4.4 23.3 1.0 CE2 A:TYR400 4.5 14.7 1.0 NZ A:LYS509 4.6 29.1 1.0 O A:HOH102 4.6 40.1 1.0 O A:SER476 4.9 23.4 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