Chlorine in PDB 1mkp: Crystal Structure of PYST1 (MKP3)

All present enzymatic activity of Crystal Structure of PYST1 (MKP3):
3.1.3.16; 3.1.3.48;

The structure of Crystal Structure of PYST1 (MKP3), PDB code: 1mkp was solved by A.E.Stewart, S.Dowd, S.Keyse, N.Q.Mcdonald, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.35
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	90.000, 90.000, 68.410, 90.00, 90.00, 90.00
R / Rfree (%)	20.1 / 23.5

The binding sites of Chlorine atom in the Crystal Structure of PYST1 (MKP3) (pdb code 1mkp). 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 PYST1 (MKP3), PDB code: 1mkp:

Chlorine binding site 1 out of 1 in the Crystal Structure of PYST1 (MKP3)


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 PYST1 (MKP3) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl500 b:41.9 occ:1.00 OG A:SER293 3.0 35.8 1.0 N A:ARG299 3.4 35.0 1.0 CB A:ARG299 3.6 34.0 1.0 CG A:ARG299 3.6 34.4 1.0 NH1 A:ARG299 3.6 36.2 1.0 N A:GLY296 3.8 40.0 1.0 CB A:SER293 3.8 37.1 1.0 O A:GLY296 3.8 40.8 1.0 C A:GLY296 3.9 39.4 1.0 CB A:ALA295 4.0 38.9 1.0 CD A:ARG299 4.0 35.2 1.0 C A:ALA295 4.0 39.5 1.0 CA A:GLY296 4.1 39.8 1.0 CA A:ARG299 4.1 33.8 1.0 N A:SER298 4.1 36.0 1.0 C A:SER298 4.4 35.4 1.0 N A:ILE297 4.4 38.4 1.0 O A:ALA295 4.4 40.6 1.0 CA A:ALA295 4.4 39.2 1.0 CA A:SER298 4.5 35.1 1.0 CB A:SER298 4.5 34.4 1.0 CZ A:ARG299 4.6 37.2 1.0 C A:ILE297 4.6 37.0 1.0 O A:HOH421 4.7 36.3 1.0 NE A:ARG299 4.8 36.8 1.0 N A:SER300 4.8 32.9 1.0 O A:HOH419 4.8 40.6 1.0 N A:ALA295 4.8 39.1 1.0 C A:ARG299 5.0 33.5 1.0 CA A:ILE297 5.0 37.1 1.0

A.E.Stewart, S.Dowd, S.M.Keyse, N.Q.Mcdonald. Crystal Structure of the Mapk Phosphatase PYST1 Catalytic Domain and Implications For Regulated Activation. Nat.Struct.Biol. V. 6 174 1999.
ISSN: ISSN 1072-8368
PubMed: 10048930
DOI: 10.1038/5861