Cobalt in PDB 1cah: Structure of Cobalt Carbonic Anhydrase Complexed with Bicarbonate

All present enzymatic activity of Structure of Cobalt Carbonic Anhydrase Complexed with Bicarbonate:
4.2.1.1;

The structure of Structure of Cobalt Carbonic Anhydrase Complexed with Bicarbonate, PDB code: 1cah was solved by K.Hakansson, A.Wehnert, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.88
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.700, 41.700, 73.000, 90.00, 104.60, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Cobalt atom in the Structure of Cobalt Carbonic Anhydrase Complexed with Bicarbonate (pdb code 1cah). 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 Structure of Cobalt Carbonic Anhydrase Complexed with Bicarbonate, PDB code: 1cah:

Cobalt binding site 1 out of 1 in the Structure of Cobalt Carbonic Anhydrase Complexed with Bicarbonate


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Structure of Cobalt Carbonic Anhydrase Complexed with Bicarbonate within 5.0Å range: probe atom residue distance (Å) B Occ A:Co262 b:9.4 occ:1.00 ND1 A:HIS119 2.1 3.0 1.0 NE2 A:HIS96 2.2 2.1 1.0 NE2 A:HIS94 2.2 6.6 1.0 O A:HOH263 2.3 23.0 1.0 O3 A:BCT500 2.4 39.1 1.0 O2 A:BCT500 2.4 38.1 1.0 C A:BCT500 2.7 39.0 1.0 CE1 A:HIS119 3.0 3.3 1.0 CD2 A:HIS94 3.0 4.1 1.0 CE1 A:HIS96 3.0 2.8 1.0 CG A:HIS119 3.2 4.2 1.0 CE1 A:HIS94 3.2 6.6 1.0 CD2 A:HIS96 3.2 3.1 1.0 CB A:HIS119 3.6 3.0 1.0 O1 A:BCT500 3.9 39.8 1.0 OG1 A:THR199 4.0 8.0 1.0 NE2 A:HIS119 4.1 2.1 1.0 OE1 A:GLU106 4.2 8.7 1.0 CG A:HIS94 4.2 5.9 1.0 ND1 A:HIS96 4.2 2.9 1.0 CD2 A:HIS119 4.2 2.7 1.0 ND1 A:HIS94 4.3 4.9 1.0 CG A:HIS96 4.3 2.6 1.0 O A:HOH292 4.3 18.6 1.0

K.Hakansson, A.Wehnert. Structure of Cobalt Carbonic Anhydrase Complexed with Bicarbonate. J.Mol.Biol. V. 228 1212 1992.
ISSN: ISSN 0022-2836
PubMed: 1474587
DOI: 10.1016/0022-2836(92)90327-G