Chlorine in PDB 2oud: Crystal Structure of the Catalytic Domain of Human MKP5

All present enzymatic activity of Crystal Structure of the Catalytic Domain of Human MKP5:
3.1.3.16; 3.1.3.48;

The structure of Crystal Structure of the Catalytic Domain of Human MKP5, PDB code: 2oud was solved by X.Tao, L.Tong, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.84 / 2.80
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	92.514, 92.514, 78.114, 90.00, 90.00, 120.00
R / Rfree (%)	21.3 / 24.8

The binding sites of Chlorine atom in the Crystal Structure of the Catalytic Domain of Human MKP5 (pdb code 2oud). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of the Catalytic Domain of Human MKP5, PDB code: 2oud:

Chlorine binding site 1 out of 1 in the Crystal Structure of the Catalytic Domain of Human MKP5


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 Catalytic Domain of Human MKP5 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1 b:66.0 occ:1.00 NH2 A:ARG414 3.2 55.3 1.0 SG A:CYS408 3.3 55.6 1.0 NE A:ARG414 3.7 57.8 1.0 N A:ALA410 3.8 57.7 1.0 CZ A:ARG414 3.9 55.3 1.0 N A:SER413 4.0 53.1 1.0 N A:GLN409 4.2 55.4 1.0 CB A:GLN409 4.3 58.7 1.0 N A:VAL412 4.3 53.3 1.0 CB A:CYS408 4.4 51.3 1.0 N A:ARG414 4.4 54.7 1.0 CB A:SER413 4.4 49.5 1.0 CB A:ALA410 4.4 52.5 1.0 N A:GLY411 4.5 58.5 1.0 CA A:ALA410 4.6 57.3 1.0 CA A:GLN409 4.6 57.6 1.0 CA A:SER413 4.7 52.9 1.0 CB A:ASP377 4.7 57.0 1.0 O A:HOH7 4.7 48.5 1.0 C A:GLN409 4.7 58.7 1.0 CB A:VAL412 4.7 51.4 1.0 CG A:ASP377 4.8 57.6 1.0 OD2 A:ASP377 4.8 60.7 1.0 CA A:VAL412 4.9 52.7 1.0 C A:ALA410 4.9 58.8 1.0 C A:VAL412 4.9 54.4 1.0 CD A:ARG414 5.0 57.3 1.0

X.Tao, L.Tong. Crystal Structure of the Map Kinase Binding Domain and the Catalytic Domain of Human MKP5. Protein Sci. V. 16 880 2007.
ISSN: ISSN 0961-8368
PubMed: 17400920
DOI: 10.1110/PS.062712807