Zinc in PDB 2fnk: Activation of Human Carbonic Anhydrase II By Exogenous Proton Donors

All present enzymatic activity of Activation of Human Carbonic Anhydrase II By Exogenous Proton Donors:
4.2.1.1;

The structure of Activation of Human Carbonic Anhydrase II By Exogenous Proton Donors, PDB code: 2fnk was solved by D.Bhatt, S.Z.Fisher, C.Tu, R.Mckenna, D.N.Silverman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.80
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.092, 41.402, 71.928, 90.00, 104.01, 90.00
R / Rfree (%)	20.4 / 24.2

The binding sites of Zinc atom in the Activation of Human Carbonic Anhydrase II By Exogenous Proton Donors (pdb code 2fnk). 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 Activation of Human Carbonic Anhydrase II By Exogenous Proton Donors, PDB code: 2fnk:

Zinc binding site 1 out of 1 in the Activation of Human Carbonic Anhydrase II By Exogenous Proton Donors


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Activation of Human Carbonic Anhydrase II By Exogenous Proton Donors within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn262 b:9.2 occ:1.00 O A:HOH297 1.9 11.1 1.0 NE2 A:HIS94 2.0 8.7 1.0 NE2 A:HIS96 2.1 7.5 1.0 ND1 A:HIS119 2.1 7.5 1.0 CD2 A:HIS94 2.9 6.9 1.0 CE1 A:HIS94 3.0 10.8 1.0 CE1 A:HIS119 3.0 5.7 1.0 CD2 A:HIS96 3.0 8.9 1.0 CE1 A:HIS96 3.0 7.2 1.0 CG A:HIS119 3.2 6.0 1.0 CB A:HIS119 3.6 6.6 1.0 OG1 A:THR199 3.7 6.9 1.0 O A:HOH302 3.9 16.8 1.0 OE1 A:GLU106 4.0 6.6 1.0 ND1 A:HIS94 4.1 6.9 1.0 CG A:HIS94 4.1 7.0 1.0 ND1 A:HIS96 4.2 7.0 1.0 NE2 A:HIS119 4.2 3.9 1.0 CG A:HIS96 4.2 5.8 1.0 CD2 A:HIS119 4.3 6.8 1.0 O A:HOH448 4.4 28.0 1.0 O A:HOH446 4.5 20.1 1.0 CD A:GLU106 4.8 6.7 1.0

D.Bhatt, S.Z.Fisher, C.Tu, R.Mckenna, D.N.Silverman. Location of Binding Sites in Small Molecule Rescue of Human Carbonic Anhydrase II. Biophys.J. V. 92 562 2007.
ISSN: ISSN 0006-3495
PubMed: 17071654
DOI: 10.1529/BIOPHYSJ.106.093203