Chlorine in PDB 2r8x: Crystal Structure of Yrbi Phosphatase From Escherichia Coli

All present enzymatic activity of Crystal Structure of Yrbi Phosphatase From Escherichia Coli:
3.1.3.45;

The structure of Crystal Structure of Yrbi Phosphatase From Escherichia Coli, PDB code: 2r8x was solved by O.V.Tsodikov, P.Aggarwal, J.R.Rubin, J.A.Stuckey, R.W.Woodard, T.Biswas, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.60
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	85.071, 156.959, 114.407, 90.00, 96.54, 90.00
R / Rfree (%)	20.1 / 23.6

The binding sites of Chlorine atom in the Crystal Structure of Yrbi Phosphatase From Escherichia Coli (pdb code 2r8x). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Crystal Structure of Yrbi Phosphatase From Escherichia Coli, PDB code: 2r8x:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the Crystal Structure of Yrbi Phosphatase From Escherichia Coli


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 Yrbi Phosphatase From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl189 b:72.7 occ:1.00 N A:GLY77 3.0 36.9 1.0 O A:HOH234 3.1 41.9 1.0 NZ A:LYS102 3.3 39.3 1.0 O A:HOH214 3.3 27.6 1.0 O A:HOH192 3.3 26.6 1.0 OD2 A:ASP32 3.4 35.9 1.0 CA A:GLY77 3.6 36.9 1.0 CE A:LYS102 3.6 39.2 1.0 O B:SER187 3.7 45.6 1.0 CB B:SER187 3.7 45.6 1.0 C A:THR76 4.1 36.9 1.0 CG A:ASP32 4.2 35.7 1.0 OG1 A:THR76 4.2 37.0 1.0 CG2 A:ILE128 4.2 36.0 1.0 CA A:THR76 4.2 36.9 1.0 OD1 A:ASP32 4.3 37.2 1.0 OG B:SER187 4.5 45.7 1.0 C B:SER187 4.5 45.5 1.0 CA B:SER187 4.6 45.6 1.0 C A:GLY77 4.7 36.9 1.0 N A:ARG78 4.8 36.9 1.0 CB A:THR76 4.8 36.9 1.0 N B:SER187 4.9 45.8 1.0

Chlorine binding site 2 out of 4 in the Crystal Structure of Yrbi Phosphatase From Escherichia Coli


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 Yrbi Phosphatase From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl189 b:73.1 occ:1.00 N B:GLY77 3.2 32.6 1.0 O C:HOH201 3.2 28.4 1.0 NZ B:LYS102 3.4 37.5 1.0 OD2 B:ASP32 3.5 30.1 1.0 O B:HOH195 3.6 35.4 1.0 O C:SER187 3.6 47.0 1.0 CE B:LYS102 3.6 37.1 1.0 CB C:SER187 3.7 47.1 1.0 CA B:GLY77 3.7 32.7 1.0 OD1 B:ASP32 4.1 32.2 1.0 CG B:ASP32 4.2 30.1 1.0 CG2 B:ILE128 4.2 31.7 1.0 C B:THR76 4.2 32.5 1.0 OG1 B:THR76 4.4 32.9 1.0 CA B:THR76 4.4 32.4 1.0 OG C:SER187 4.4 47.3 1.0 C C:SER187 4.5 47.0 1.0 CA C:SER187 4.5 47.1 1.0 N C:SER187 4.8 47.5 1.0 C B:GLY77 4.8 32.9 1.0 N B:ARG78 4.9 32.8 1.0 CB B:THR76 5.0 32.5 1.0

Chlorine binding site 3 out of 4 in the Crystal Structure of Yrbi Phosphatase From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of Yrbi Phosphatase From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl189 b:78.0 occ:1.00 N C:GLY77 3.0 36.2 1.0 O C:HOH244 3.3 39.0 1.0 O C:HOH238 3.3 42.2 1.0 NZ C:LYS102 3.4 44.5 1.0 O C:HOH195 3.4 30.0 1.0 CA C:GLY77 3.5 36.3 1.0 OD2 C:ASP32 3.5 36.3 1.0 CB D:SER187 3.6 55.8 1.0 CE C:LYS102 3.9 44.0 1.0 O D:SER187 3.9 55.8 1.0 C C:THR76 4.0 36.0 1.0 OG D:SER187 4.1 55.7 1.0 CG2 C:ILE128 4.2 35.1 1.0 CA C:THR76 4.3 35.8 1.0 OG1 C:THR76 4.3 36.2 1.0 CG C:ASP32 4.4 35.3 1.0 OD1 C:ASP32 4.4 35.8 1.0 CA D:SER187 4.6 55.8 1.0 C C:GLY77 4.7 36.4 1.0 C D:SER187 4.7 55.8 1.0 N C:ARG78 4.8 36.4 1.0 CB C:THR76 4.9 35.9 1.0 N D:SER187 4.9 55.7 1.0

Chlorine binding site 4 out of 4 in the Crystal Structure of Yrbi Phosphatase From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Crystal Structure of Yrbi Phosphatase From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ G:Cl189 b:82.6 occ:1.00 O G:HOH230 3.1 51.2 1.0 N G:GLY77 3.1 36.7 1.0 OD2 G:ASP32 3.3 33.0 1.0 NZ G:LYS102 3.3 38.1 1.0 O G:HOH198 3.4 40.1 1.0 CB H:SER187 3.6 49.4 1.0 CE G:LYS102 3.7 37.7 1.0 CA G:GLY77 3.7 36.9 1.0 O H:SER187 3.7 49.3 1.0 CG G:ASP32 4.1 32.2 1.0 OD1 G:ASP32 4.1 33.6 1.0 C G:THR76 4.1 36.5 1.0 CA G:THR76 4.2 36.3 1.0 OG1 G:THR76 4.3 36.8 1.0 OG H:SER187 4.3 49.8 1.0 CG2 G:ILE128 4.4 32.2 1.0 CA H:SER187 4.5 49.4 1.0 C H:SER187 4.5 49.3 1.0 C G:GLY77 4.8 36.9 1.0 N H:SER187 4.8 49.6 1.0 CB G:THR76 4.9 36.4 1.0 N G:ARG78 4.9 37.0 1.0

T.Biswas, L.Yi, P.Aggarwal, J.Wu, J.R.Rubin, J.A.Stuckey, R.W.Woodard, O.V.Tsodikov. The Tail of Kdsc: Conformational Changes Control the Activity of A Haloacid Dehalogenase Superfamily Phosphatase. J.Biol.Chem. V. 284 30594 2009.
ISSN: ISSN 0021-9258
PubMed: 19726684
DOI: 10.1074/JBC.M109.012278