Chlorine in PDB 2v5g: Crystal Structure of the Mutated N263A Yscu C-Terminal Domain

The structure of Crystal Structure of the Mutated N263A Yscu C-Terminal Domain, PDB code: 2v5g was solved by U.Wiesand, I.Sorg, M.Amstutz, S.Wagner, J.Van Den Heuvel, T.Luehrs, G.R.Cornelis, D.W.Heinz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.84 / 2.00
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	66.297, 66.297, 68.500, 90.00, 90.00, 90.00
R / Rfree (%)	22.1 / 25.3

The binding sites of Chlorine atom in the Crystal Structure of the Mutated N263A Yscu C-Terminal Domain (pdb code 2v5g). 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 the Mutated N263A Yscu C-Terminal Domain, PDB code: 2v5g:

Chlorine binding site 1 out of 1 in the Crystal Structure of the Mutated N263A Yscu C-Terminal Domain


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 the Mutated N263A Yscu C-Terminal Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1342 b:26.9 occ:1.00 N A:TYR225 3.0 48.7 1.0 O A:HOH2004 3.1 37.8 1.0 CA A:GLU224 3.7 45.6 1.0 CB A:TYR225 3.7 51.2 1.0 C A:GLU224 3.8 47.5 1.0 CB A:TYR325 3.8 20.8 1.0 CD2 A:TYR325 3.8 23.6 1.0 CA A:TYR225 3.9 51.0 1.0 CG A:GLU224 4.1 47.1 1.0 CD1 A:LEU280 4.1 18.3 1.0 CB A:GLU224 4.2 46.0 1.0 CG A:TYR325 4.3 24.7 1.0 N A:LYS226 4.3 54.7 1.0 CD A:GLU224 4.6 47.2 1.0 O A:ARG223 4.6 41.3 0.5 O A:ARG223 4.6 41.6 0.5 C A:TYR225 4.7 53.0 1.0 N A:GLU224 4.8 44.4 1.0 CA A:TYR325 4.9 19.4 1.0 O A:TYR325 4.9 19.2 1.0 OE2 A:GLU224 5.0 46.2 1.0 O A:GLU224 5.0 49.0 1.0 CE2 A:TYR325 5.0 26.1 1.0

U.Wiesand, I.Sorg, M.Amstutz, S.Wagner, J.Van Den Heuvel, T.Luehrs, G.R.Cornelis, D.W.Heinz. Structure of the Type III Secretion Recognition Protein Yscu From Yersinia Enterocolitica J.Mol.Biol. V. 385 854 2009.
ISSN: ISSN 0022-2836
PubMed: 18976663
DOI: 10.1016/J.JMB.2008.10.034