Chlorine in PDB 7o4z: Crystal Structure of the Carbonic Anhydrase-Like Domain of Ccmm From Synechococcus Elongatus (Strain Pcc 7942)

The structure of Crystal Structure of the Carbonic Anhydrase-Like Domain of Ccmm From Synechococcus Elongatus (Strain Pcc 7942), PDB code: 7o4z was solved by K.Zang, H.Wang, F.U.Hartl, M.Hayer-Hartl, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	66.81 / 1.67
Space group	H 3 2
Cell size a, b, c (Å), α, β, γ (°)	89.741, 89.741, 130.79, 90, 90, 120
R / Rfree (%)	16.4 / 20

The structure of Crystal Structure of the Carbonic Anhydrase-Like Domain of Ccmm From Synechococcus Elongatus (Strain Pcc 7942) also contains other interesting chemical elements:

Nickel

(Ni)

1 atom

The binding sites of Chlorine atom in the Crystal Structure of the Carbonic Anhydrase-Like Domain of Ccmm From Synechococcus Elongatus (Strain Pcc 7942) (pdb code 7o4z). 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 Carbonic Anhydrase-Like Domain of Ccmm From Synechococcus Elongatus (Strain Pcc 7942), PDB code: 7o4z:

Chlorine binding site 1 out of 1 in the Crystal Structure of the Carbonic Anhydrase-Like Domain of Ccmm From Synechococcus Elongatus (Strain Pcc 7942)


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 Carbonic Anhydrase-Like Domain of Ccmm From Synechococcus Elongatus (Strain Pcc 7942) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl202 b:24.5 occ:0.33 O A:HOH387 2.7 40.0 1.0 NH1 A:ARG119 3.2 20.0 1.0 CG A:ARG119 3.7 20.8 1.0 CD A:ARG119 3.9 18.1 1.0 CZ A:ARG119 4.2 19.7 1.0 NE A:ARG119 4.5 18.1 1.0 CD A:LYS101 4.5 22.9 1.0 O A:HOH415 4.7 24.3 0.3 CB A:LYS101 4.8 19.5 1.0

K.Zang, H.Wang, F.U.Hartl, M.Hayer-Hartl. Multiplicity of Protein-Protein Interactions Directing Condensate Formation in Beta-Carboxysome Biogenesis To Be Published.