Chlorine in PDB 2yhg: Ab Initio Phasing of A Nucleoside Hydrolase-Related Hypothetical Protein From Saccharophagus Degradans That Is Associated with Carbohydrate Metabolism

The structure of Ab Initio Phasing of A Nucleoside Hydrolase-Related Hypothetical Protein From Saccharophagus Degradans That Is Associated with Carbohydrate Metabolism, PDB code: 2yhg was solved by J.H.Hehemann, C.Marsters, A.B.Boraston, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	62.73 / 1.08
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	54.580, 61.580, 125.460, 90.00, 90.00, 90.00
R / Rfree (%)	13.3 / 15.1

The structure of Ab Initio Phasing of A Nucleoside Hydrolase-Related Hypothetical Protein From Saccharophagus Degradans That Is Associated with Carbohydrate Metabolism also contains other interesting chemical elements:

Calcium	(Ca)	2 atoms
Zinc	(Zn)	1 atom
Magnesium	(Mg)	3 atoms

The binding sites of Chlorine atom in the Ab Initio Phasing of A Nucleoside Hydrolase-Related Hypothetical Protein From Saccharophagus Degradans That Is Associated with Carbohydrate Metabolism (pdb code 2yhg). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Ab Initio Phasing of A Nucleoside Hydrolase-Related Hypothetical Protein From Saccharophagus Degradans That Is Associated with Carbohydrate Metabolism, PDB code: 2yhg:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Ab Initio Phasing of A Nucleoside Hydrolase-Related Hypothetical Protein From Saccharophagus Degradans That Is Associated with Carbohydrate Metabolism


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Ab Initio Phasing of A Nucleoside Hydrolase-Related Hypothetical Protein From Saccharophagus Degradans That Is Associated with Carbohydrate Metabolism within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1935 b:11.3 occ:1.00 OH A:TYR875 3.1 10.7 1.0 NE A:ARG766 3.2 10.4 1.0 NH1 A:ARG802 3.2 14.7 1.0 MG A:MG1939 3.4 11.0 0.7 CD A:ARG802 3.6 13.3 1.0 CB A:SER799 3.7 8.1 1.0 CD A:ARG766 3.8 8.9 1.0 CE1 A:TYR875 3.9 9.8 1.0 CZ A:TYR875 3.9 9.4 1.0 CB A:ARG766 4.0 7.3 1.0 CZ A:ARG802 4.2 15.3 1.0 CZ A:ARG766 4.2 11.2 1.0 NE A:ARG802 4.3 14.7 1.0 NH2 A:ARG766 4.3 14.4 1.0 CA A:SER799 4.4 8.0 1.0 O A:SER799 4.5 9.1 1.0 CG A:ARG766 4.5 7.5 1.0 OE2 A:GLU877 4.8 17.9 1.0 CB A:GLU877 4.9 12.9 1.0 C A:SER799 4.9 7.2 1.0 CG A:ARG802 4.9 10.3 1.0 OG A:SER799 4.9 8.1 1.0 O A:HOH2390 5.0 31.6 1.0 CD A:GLU877 5.0 16.8 1.0

Chlorine binding site 2 out of 2 in the Ab Initio Phasing of A Nucleoside Hydrolase-Related Hypothetical Protein From Saccharophagus Degradans That Is Associated with Carbohydrate Metabolism


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Ab Initio Phasing of A Nucleoside Hydrolase-Related Hypothetical Protein From Saccharophagus Degradans That Is Associated with Carbohydrate Metabolism within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1940 b:9.7 occ:0.70 OG A:SER705 3.0 15.5 0.5 OG A:SER708 3.0 10.8 1.0 N A:TYR707 3.3 7.7 1.0 C A:SER705 3.3 6.9 1.0 CA A:SER705 3.5 6.5 0.5 CA A:SER705 3.5 7.1 0.5 N A:VAL706 3.6 6.8 1.0 N A:SER708 3.7 8.1 1.0 O A:SER705 3.7 7.7 1.0 CB A:TYR707 3.7 8.6 1.0 CA A:TYR707 3.8 7.8 1.0 CB A:SER705 3.8 8.6 0.5 CB A:SER705 3.9 6.9 0.5 O A:HOH2181 3.9 8.4 1.0 CB A:SER708 3.9 9.2 1.0 C A:TYR707 3.9 8.2 1.0 CG A:GLU798 4.1 11.1 1.0 C A:VAL706 4.3 7.0 1.0 CA A:SER708 4.4 8.7 1.0 OG A:SER705 4.5 7.0 0.5 CA A:VAL706 4.5 7.0 1.0 CD2 A:TYR707 4.6 9.5 1.0 CG A:TYR707 4.6 9.0 1.0 O A:ARG704 4.7 8.4 1.0 O A:TYR707 4.8 9.6 1.0 N A:SER705 4.8 6.7 1.0 CB A:GLU798 4.9 10.7 1.0

J.H.Hehemann, C.Marsters, A.B.Boraston. Ab Initio Phasing of A Nucleoside Hydrolase-Related Hypothetical Protein From Saccharophagus Degradans That Is Associated with Carbohydrate Metabolism. Proteins V. 79 2992 2011.
ISSN: ESSN 1097-0134
PubMed: 21905122
DOI: 10.1002/PROT.23126