Zinc in PDB 3d92: Human Carbonic Anhydrase II Bound with Substrate Carbon Dioxide

All present enzymatic activity of Human Carbonic Anhydrase II Bound with Substrate Carbon Dioxide:
4.2.1.1;

The structure of Human Carbonic Anhydrase II Bound with Substrate Carbon Dioxide, PDB code: 3d92 was solved by J.F.Domsic, B.S.Avvaru, R.Mckenna, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.10
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 (%)	10 / 12.9

The binding sites of Zinc atom in the Human Carbonic Anhydrase II Bound with Substrate Carbon Dioxide (pdb code 3d92). 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 Bound with Substrate Carbon Dioxide, PDB code: 3d92:

Zinc binding site 1 out of 1 in the Human Carbonic Anhydrase II Bound with Substrate Carbon Dioxide


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 Bound with Substrate Carbon Dioxide within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn262 b:5.0 occ:1.00 O A:HOH401 1.9 9.3 1.0 NE2 A:HIS94 2.0 4.5 1.0 NE2 A:HIS96 2.0 5.0 1.0 ND1 A:HIS119 2.0 4.7 1.0 CE1 A:HIS119 2.9 4.5 1.0 CD2 A:HIS94 3.0 4.9 1.0 CE1 A:HIS94 3.0 5.0 1.0 CD2 A:HIS96 3.0 4.7 1.0 CE1 A:HIS96 3.1 6.2 1.0 CG A:HIS119 3.2 4.4 1.0 O1 A:CO2301 3.3 12.6 1.0 CB A:HIS119 3.6 4.5 1.0 C A:CO2301 3.7 11.8 1.0 OG1 A:THR199 3.8 5.7 1.0 OE1 A:GLU106 4.0 5.8 1.0 CG A:HIS94 4.1 4.6 1.0 ND1 A:HIS94 4.1 4.9 1.0 NE2 A:HIS119 4.1 4.8 1.0 ND1 A:HIS96 4.2 5.9 1.0 CG A:HIS96 4.2 4.8 1.0 CD2 A:HIS119 4.2 4.8 1.0 O A:HOH592 4.4 26.5 1.0 O2 A:CO2301 4.5 17.5 1.0 C3 A:GOL303 4.6 15.7 1.0 CD A:GLU106 4.9 5.2 1.0

J.F.Domsic, B.S.Avvaru, C.U.Kim, S.M.Gruner, M.Agbandje-Mckenna, D.N.Silverman, R.Mckenna. Entrapment of Carbon Dioxide in the Active Site of Carbonic Anhydrase II J.Biol.Chem. V. 283 30766 2008.
ISSN: ISSN 0021-9258
PubMed: 18768466
DOI: 10.1074/JBC.M805353200