Cobalt in PDB 4mag: Crystal Structure of the Periplasmic Sialic Acid Binding Protein From Vibrio Cholerea

The structure of Crystal Structure of the Periplasmic Sialic Acid Binding Protein From Vibrio Cholerea, PDB code: 4mag was solved by S.Ramaswamy, C.Cho, M.A.Apicella, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	11.73 / 1.45
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	74.977, 82.315, 119.354, 90.00, 90.00, 90.00
R / Rfree (%)	18.2 / 21.9

The binding sites of Cobalt atom in the Crystal Structure of the Periplasmic Sialic Acid Binding Protein From Vibrio Cholerea (pdb code 4mag). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total only one binding site of Cobalt was determined in the Crystal Structure of the Periplasmic Sialic Acid Binding Protein From Vibrio Cholerea, PDB code: 4mag:

Cobalt binding site 1 out of 1 in the Crystal Structure of the Periplasmic Sialic Acid Binding Protein From Vibrio Cholerea


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Crystal Structure of the Periplasmic Sialic Acid Binding Protein From Vibrio Cholerea within 5.0Å range: probe atom residue distance (Å) B Occ A:Co401 b:30.4 occ:1.00 NE2 A:HIS307 1.9 29.4 1.0 ND1 A:HIS305 2.0 28.4 1.0 ND1 A:HIS302 2.2 33.5 1.0 CE1 A:HIS307 2.9 31.2 1.0 CE1 A:HIS305 2.9 28.4 1.0 CD2 A:HIS307 3.0 29.1 1.0 CG A:HIS305 3.0 27.4 1.0 CE1 A:HIS302 3.1 33.9 1.0 CG A:HIS302 3.2 31.8 1.0 CB A:HIS305 3.4 26.9 1.0 CB A:HIS302 3.5 29.6 1.0 CA A:HIS302 3.9 29.0 1.0 ND1 A:HIS307 4.0 32.2 1.0 NE2 A:HIS305 4.0 28.6 1.0 CD2 A:HIS305 4.1 28.0 1.0 CG A:HIS307 4.1 32.0 1.0 NE2 A:HIS302 4.1 35.6 1.0 CD2 A:HIS302 4.2 34.6 1.0 O A:HIS302 4.7 27.0 1.0 C A:HIS302 4.8 27.4 1.0 CA A:HIS305 4.9 27.4 1.0 O A:GLN301 4.9 32.3 1.0

T.Gangi Setty, C.Cho, S.Govindappa, M.A.Apicella, S.Ramaswamy. Bacterial Periplasmic Sialic Acid-Binding Proteins Exhibit A Conserved Binding Site. Acta Crystallogr.,Sect.D V. 70 1801 2014.
ISSN: ISSN 0907-4449
PubMed: 25004958
DOI: 10.1107/S139900471400830X