Cobalt in PDB 3koi: Crystal Structure of Cobalt (III) Human Carbonic Anhydrase II at pH 6.0

All present enzymatic activity of Crystal Structure of Cobalt (III) Human Carbonic Anhydrase II at pH 6.0:
4.2.1.1;

The structure of Crystal Structure of Cobalt (III) Human Carbonic Anhydrase II at pH 6.0, PDB code: 3koi was solved by B.S.Avvaru, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.64
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.422, 41.563, 72.993, 90.00, 105.53, 90.00
R / Rfree (%)	22 / 21.5

The binding sites of Cobalt atom in the Crystal Structure of Cobalt (III) Human Carbonic Anhydrase II at pH 6.0 (pdb code 3koi). 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 Cobalt (III) Human Carbonic Anhydrase II at pH 6.0, PDB code: 3koi:

Cobalt binding site 1 out of 1 in the Crystal Structure of Cobalt (III) Human Carbonic Anhydrase II at pH 6.0


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 Cobalt (III) Human Carbonic Anhydrase II at pH 6.0 within 5.0Å range: probe atom residue distance (Å) B Occ A:Co262 b:8.1 occ:1.00 NE2 A:HIS94 2.0 5.9 1.0 ND1 A:HIS119 2.1 2.2 1.0 O A:HOH267 2.2 6.2 1.0 NE2 A:HIS96 2.2 0.0 1.0 O A:HOH375 2.3 22.6 1.0 O A:HOH272 2.4 4.2 1.0 CE1 A:HIS94 2.9 10.8 1.0 CD2 A:HIS94 3.0 4.2 1.0 CE1 A:HIS119 3.0 0.0 1.0 CD2 A:HIS96 3.1 5.0 1.0 CG A:HIS119 3.2 2.5 1.0 CE1 A:HIS96 3.3 3.4 1.0 CB A:HIS119 3.6 0.0 1.0 OG1 A:THR199 3.9 3.0 1.0 OE1 A:GLU106 4.0 5.4 1.0 ND1 A:HIS94 4.1 3.2 1.0 CG A:HIS94 4.1 0.3 1.0 NE2 A:HIS119 4.2 2.5 1.0 CD2 A:HIS119 4.3 7.5 1.0 CG A:HIS96 4.3 2.4 1.0 ND1 A:HIS96 4.4 1.1 1.0 O A:HOH305 4.6 15.6 1.0 CD A:GLU106 4.9 6.5 1.0

B.S.Avvaru, D.J.Arenas, C.Tu, D.B.Tanner, R.Mckenna, D.N.Silverman. Comparison of Solution and Crystal Properties of Co(II)-Substituted Human Carbonic Anhydrase II. Arch.Biochem.Biophys. V. 502 53 2010.
ISSN: ISSN 0003-9861
PubMed: 20637176
DOI: 10.1016/J.ABB.2010.07.010