Zinc in PDB 2vvb: Human Carbonic Anhydrase II in Complex with Bicarbonate

All present enzymatic activity of Human Carbonic Anhydrase II in Complex with Bicarbonate:
4.2.1.1;

The structure of Human Carbonic Anhydrase II in Complex with Bicarbonate, PDB code: 2vvb was solved by B.Sjoeblom, M.Polentarutti, K.Djinovic-Carugo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	70.71 / 1.66
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.667, 41.653, 72.910, 90.00, 104.79, 90.00
R / Rfree (%)	16.8 / 21.3

The binding sites of Zinc atom in the Human Carbonic Anhydrase II in Complex with Bicarbonate (pdb code 2vvb). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Human Carbonic Anhydrase II in Complex with Bicarbonate, PDB code: 2vvb:

Zinc binding site 1 out of 1 in the Human Carbonic Anhydrase II in Complex with Bicarbonate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Carbonic Anhydrase II in Complex with Bicarbonate within 5.0Å range: probe atom residue distance (Å) B Occ X:Zn1268 b:13.9 occ:1.00 NE2 X:HIS96 2.0 8.9 1.0 O3 X:BCT1263 2.0 16.3 1.0 NE2 X:HIS94 2.0 9.4 1.0 ND1 X:HIS119 2.1 9.1 1.0 C X:BCT1263 2.8 21.8 1.0 O1 X:BCT1263 2.9 21.4 1.0 CD2 X:HIS96 2.9 8.6 1.0 CE1 X:HIS119 2.9 7.7 1.0 CD2 X:HIS94 2.9 9.7 1.0 CE1 X:HIS96 3.0 10.1 1.0 CE1 X:HIS94 3.1 12.0 1.0 O X:HOH2299 3.1 32.9 1.0 CG X:HIS119 3.1 7.8 1.0 CB X:HIS119 3.6 9.6 1.0 OG1 X:THR199 3.8 10.6 1.0 O2 X:BCT1263 4.0 24.1 1.0 OE1 X:GLU106 4.0 14.4 1.0 ND1 X:HIS96 4.1 11.8 1.0 CG X:HIS96 4.1 7.7 1.0 NE2 X:HIS119 4.1 9.9 1.0 CG X:HIS94 4.1 8.8 1.0 ND1 X:HIS94 4.1 11.4 1.0 CD2 X:HIS119 4.2 7.0 1.0 O X:HOH2097 4.4 20.7 1.0 O X:HOH2230 4.7 29.3 1.0 O X:HOH2298 4.9 29.2 1.0 CD X:GLU106 4.9 13.4 1.0

B.Sjoblom, M.Polentarutti, K.Djinovic-Carugo. Structural Study of X-Ray Induced Activation of Carbonic Anhydrase. Proc.Natl.Acad.Sci.Usa V. 106 10609 2009.
ISSN: ISSN 0027-8424
PubMed: 19520834
DOI: 10.1073/PNAS.0904184106