Chlorine in PDB 3o6z: Structure of the D152A E.Coli Gdp-Mannose Hydrolase (Yffh) in Complex with Mg++

The structure of Structure of the D152A E.Coli Gdp-Mannose Hydrolase (Yffh) in Complex with Mg++, PDB code: 3o6z was solved by L.M.Amzel, S.B.Gabelli, A.N.Boto, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.47 / 2.05
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	58.916, 69.333, 99.612, 90.00, 90.00, 90.00
R / Rfree (%)	23.5 / 30.3

The structure of Structure of the D152A E.Coli Gdp-Mannose Hydrolase (Yffh) in Complex with Mg++ also contains other interesting chemical elements:

Magnesium

(Mg)

3 atoms

The binding sites of Chlorine atom in the Structure of the D152A E.Coli Gdp-Mannose Hydrolase (Yffh) in Complex with Mg++ (pdb code 3o6z). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Structure of the D152A E.Coli Gdp-Mannose Hydrolase (Yffh) in Complex with Mg++, PDB code: 3o6z:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Structure of the D152A E.Coli Gdp-Mannose Hydrolase (Yffh) in Complex with Mg++


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of the D152A E.Coli Gdp-Mannose Hydrolase (Yffh) in Complex with Mg++ within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl204 b:59.0 occ:1.00 NH1 B:ARG113 3.5 51.1 1.0 CD2 B:LEU189 3.8 32.5 1.0 CD1 B:LEU189 4.0 30.1 1.0 CZ B:ARG113 4.0 48.4 1.0 CD B:ARG113 4.0 39.5 1.0 NE B:ARG113 4.2 45.6 1.0 CG B:LEU189 4.3 30.1 1.0 O B:HOH200 4.3 45.9 1.0 O B:HOH224 4.8 46.5 1.0 NH2 B:ARG113 4.9 50.1 1.0

Chlorine binding site 2 out of 2 in the Structure of the D152A E.Coli Gdp-Mannose Hydrolase (Yffh) in Complex with Mg++


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Structure of the D152A E.Coli Gdp-Mannose Hydrolase (Yffh) in Complex with Mg++ within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl203 b:80.3 occ:1.00 CG2 B:THR28 3.6 48.8 1.0 CB B:GLN4 3.6 44.0 1.0 NE2 B:GLN3 3.9 56.1 1.0 O B:HOH277 3.9 55.1 1.0 CB B:THR28 4.1 46.2 1.0 N B:GLN4 4.4 44.9 1.0 CB B:GLN3 4.5 50.3 1.0 OG1 B:THR28 4.5 45.5 1.0 CG B:GLN4 4.6 45.2 1.0 CD B:GLN3 4.6 54.3 1.0 CA B:GLN4 4.7 43.1 1.0 CG B:GLN3 4.8 52.4 1.0

A.N.Boto, W.Xu, J.Jakoncic, A.Pannuri, T.Romeo, M.J.Bessman, S.B.Gabelli, L.M.Amzel. Structural Studies of the Nudix Gdp-Mannose Hydrolase From E. Coli Reveals A New Motif For Mannose Recognition. Proteins V. 79 2455 2011.
ISSN: ISSN 0887-3585
PubMed: 21638333
DOI: 10.1002/PROT.23069