Zinc in PDB 1yo2: Proton Transfer From HIS200 in Human Carbonic Anhydrase II

All present enzymatic activity of Proton Transfer From HIS200 in Human Carbonic Anhydrase II:
4.2.1.1;

The structure of Proton Transfer From HIS200 in Human Carbonic Anhydrase II, PDB code: 1yo2 was solved by D.Bhatt, C.Tu, S.Z.Fisher, J.A.Hernandez Prada, 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 (°)	42.604, 41.535, 72.729, 90.00, 104.44, 90.00
R / Rfree (%)	16.8 / 20.1

The binding sites of Zinc atom in the Proton Transfer From HIS200 in Human Carbonic Anhydrase II (pdb code 1yo2). 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 Proton Transfer From HIS200 in Human Carbonic Anhydrase II, PDB code: 1yo2:

Zinc binding site 1 out of 1 in the Proton Transfer From HIS200 in Human Carbonic Anhydrase II


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Proton Transfer From HIS200 in Human Carbonic Anhydrase II within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn262 b:12.1 occ:1.00 ND1 A:HIS119 2.0 8.3 1.0 NE2 A:HIS96 2.0 9.8 1.0 NE2 A:HIS94 2.0 11.4 1.0 O A:HOH353 2.0 17.1 1.0 CE1 A:HIS119 2.8 8.8 1.0 CD2 A:HIS96 2.9 9.2 1.0 CD2 A:HIS94 3.0 10.7 1.0 CE1 A:HIS94 3.0 12.3 1.0 CE1 A:HIS96 3.0 8.5 1.0 CG A:HIS119 3.1 8.5 1.0 CB A:HIS119 3.6 7.5 1.0 OG1 A:THR199 3.8 10.0 1.0 OE1 A:GLU106 4.0 9.0 1.0 NE2 A:HIS119 4.0 6.8 1.0 O A:HOH338 4.0 27.2 1.0 CG A:HIS96 4.1 7.5 1.0 ND1 A:HIS96 4.1 8.9 1.0 ND1 A:HIS94 4.1 10.7 1.0 CG A:HIS94 4.1 9.7 1.0 CD2 A:HIS119 4.1 8.7 1.0 O A:HOH387 4.3 39.2 1.0 ND1 A:HIS200 4.5 27.3 1.0 O A:HOH396 4.7 40.3 1.0 CE1 A:HIS200 4.7 29.4 1.0 CD A:GLU106 4.9 10.7 1.0

D.Bhatt, C.Tu, S.Z.Fisher, J.A.Hernandez Prada, R.Mckenna, D.N.Silverman. Proton Transfer in A THR200HIS Mutant of Human Carbonic Anhydrase II Proteins V. 61 239 2005.
ISSN: ISSN 0887-3585
PubMed: 16106378
DOI: 10.1002/PROT.20615