Zinc in PDB 3ks3: High Resolution Structure of Human Carbonic Anhydrase II at 0.9 A

All present enzymatic activity of High Resolution Structure of Human Carbonic Anhydrase II at 0.9 A:
4.2.1.1;

The structure of High Resolution Structure of Human Carbonic Anhydrase II at 0.9 A, PDB code: 3ks3 was solved by B.S.Avvaru, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.83 / 0.90
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.354, 41.359, 72.308, 90.00, 104.42, 90.00
R / Rfree (%)	13.8 / 14.5

The binding sites of Zinc atom in the High Resolution Structure of Human Carbonic Anhydrase II at 0.9 A (pdb code 3ks3). 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 High Resolution Structure of Human Carbonic Anhydrase II at 0.9 A, PDB code: 3ks3:

Zinc binding site 1 out of 1 in the High Resolution Structure of Human Carbonic Anhydrase II at 0.9 A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of High Resolution Structure of Human Carbonic Anhydrase II at 0.9 A within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn262 b:5.6 occ:1.00 O A:HOH402 1.9 8.0 0.9 ND1 A:HIS119 2.0 6.0 1.0 NE2 A:HIS94 2.0 5.9 1.0 NE2 A:HIS96 2.0 6.0 1.0 O A:HOH707 2.6 13.0 0.3 CE1 A:HIS119 2.9 5.9 1.0 CD2 A:HIS94 3.0 5.9 1.0 CD2 A:HIS96 3.0 6.0 1.0 CE1 A:HIS96 3.0 6.8 1.0 CE1 A:HIS94 3.0 6.2 1.0 CG A:HIS119 3.1 5.5 1.0 CB A:HIS119 3.6 5.5 1.0 O A:HOH512 3.7 9.6 0.7 OG1 A:THR199 3.8 6.5 1.0 O A:HOH541 4.0 18.4 0.8 OE1 A:GLU106 4.0 6.7 1.0 NE2 A:HIS119 4.1 6.2 1.0 ND1 A:HIS94 4.1 6.1 1.0 ND1 A:HIS96 4.1 7.0 1.0 CG A:HIS94 4.2 5.6 1.0 CG A:HIS96 4.2 5.9 1.0 CD2 A:HIS119 4.2 5.7 1.0 O A:HOH558 4.4 14.7 0.7 CD A:GLU106 4.9 6.2 1.0

B.S.Avvaru, C.U.Kim, K.H.Sippel, S.M.Gruner, M.Agbandje-Mckenna, D.N.Silverman, R.Mckenna. A Short, Strong Hydrogen Bond in the Active Site of Human Carbonic Anhydrase II. Biochemistry V. 49 249 2010.
ISSN: ISSN 0006-2960
PubMed: 20000378
DOI: 10.1021/BI902007B