Chlorine in PDB 2r6o: Crystal Structure of Putative Diguanylate Cyclase/Phosphodiesterase From Thiobacillus Denitrificans

The structure of Crystal Structure of Putative Diguanylate Cyclase/Phosphodiesterase From Thiobacillus Denitrificans, PDB code: 2r6o was solved by C.Chang, X.Xu, H.Zheng, A.Savchenko, A.M.Edwards, A.Joachimiak, Midwestcenter For Structural Genomics (Mcsg), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	27.70 / 1.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	50.051, 63.141, 173.282, 90.00, 90.00, 90.00
R / Rfree (%)	18.8 / 21.8

The structure of Crystal Structure of Putative Diguanylate Cyclase/Phosphodiesterase From Thiobacillus Denitrificans also contains other interesting chemical elements:

Magnesium

(Mg)

3 atoms

The binding sites of Chlorine atom in the Crystal Structure of Putative Diguanylate Cyclase/Phosphodiesterase From Thiobacillus Denitrificans (pdb code 2r6o). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Crystal Structure of Putative Diguanylate Cyclase/Phosphodiesterase From Thiobacillus Denitrificans, PDB code: 2r6o:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Crystal Structure of Putative Diguanylate Cyclase/Phosphodiesterase From Thiobacillus Denitrificans


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 Putative Diguanylate Cyclase/Phosphodiesterase From Thiobacillus Denitrificans within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl804 b:30.9 occ:1.00 O A:HOH4 3.2 21.8 1.0 O A:HOH373 3.3 37.7 1.0 N A:VAL526 3.3 24.5 1.0 ND2 A:ASN584 3.5 26.6 1.0 CG1 A:VAL526 3.8 25.3 1.0 CA A:LEU525 3.9 24.4 1.0 CB A:ASN584 4.0 25.6 1.0 O A:ALA524 4.0 25.4 1.0 CB A:VAL526 4.1 24.2 1.0 C A:LEU525 4.1 24.3 1.0 CG A:ASN584 4.2 26.3 1.0 CA A:VAL526 4.3 23.8 1.0 N A:LEU525 4.7 25.0 1.0 C A:ALA524 4.7 25.1 1.0 CG1 A:VAL558 4.8 23.4 1.0 CD2 A:LEU525 4.9 26.6 1.0 O A:HOH56 4.9 30.0 1.0 CB A:LEU525 5.0 25.2 1.0 O A:HOH32 5.0 27.9 1.0 N A:ASN584 5.0 25.3 1.0

Chlorine binding site 2 out of 3 in the Crystal Structure of Putative Diguanylate Cyclase/Phosphodiesterase From Thiobacillus Denitrificans


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 Putative Diguanylate Cyclase/Phosphodiesterase From Thiobacillus Denitrificans within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl805 b:24.0 occ:1.00 O A:HOH7 3.2 23.1 1.0 N A:SER539 3.5 22.3 1.0 CD A:PRO538 3.5 21.3 1.0 CB A:SER539 3.6 22.9 1.0 OG A:SER539 3.6 23.7 1.0 CG A:PRO538 3.7 21.4 1.0 CE A:MSE537 3.7 24.9 1.0 CB A:MSE537 3.9 21.7 1.0 N A:PRO538 4.0 22.0 1.0 CA A:SER539 4.1 23.1 1.0 O A:HOH56 4.4 30.0 1.0 C A:PRO538 4.4 23.0 1.0 C A:MSE537 4.5 21.6 1.0 CA A:PRO538 4.6 22.5 1.0 CB A:PRO538 4.6 22.8 1.0 CG A:MSE537 4.7 22.2 1.0 CA A:MSE537 4.7 21.3 1.0 SE A:MSE537 4.8 26.6 1.0

Chlorine binding site 3 out of 3 in the Crystal Structure of Putative Diguanylate Cyclase/Phosphodiesterase From Thiobacillus Denitrificans


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 Putative Diguanylate Cyclase/Phosphodiesterase From Thiobacillus Denitrificans within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl806 b:25.8 occ:1.00 O A:HOH16 3.1 25.3 1.0 O A:HOH69 3.1 31.9 1.0 O A:HOH8 3.2 23.3 1.0 NE A:ARG609 3.3 29.2 1.0 CD A:ARG609 4.0 29.3 1.0 NH2 A:ARG609 4.2 32.7 1.0 CZ A:ARG609 4.2 30.8 1.0 CG A:ARG609 4.2 26.4 1.0 OE1 A:GLN570 4.5 23.0 1.0 NH1 A:ARG567 4.8 22.8 1.0 O A:GLY607 4.9 25.4 1.0

A.Tchigvintsev, X.Xu, A.Singer, C.Chang, G.Brown, M.Proudfoot, H.Cui, R.Flick, W.F.Anderson, A.Joachimiak, M.Y.Galperin, A.Savchenko, A.F.Yakunin. Structural Insight Into the Mechanism of C-Di-Gmp Hydrolysis By Eal Domain Phosphodiesterases. J.Mol.Biol. V. 402 524 2010.
ISSN: ISSN 0022-2836
PubMed: 20691189
DOI: 10.1016/J.JMB.2010.07.050