Zinc in PDB 2ili: Refine Atomic Structure of Human Carbonic Anhydrase II

All present enzymatic activity of Refine Atomic Structure of Human Carbonic Anhydrase II:
4.2.1.1;

The structure of Refine Atomic Structure of Human Carbonic Anhydrase II, PDB code: 2ili was solved by S.Z.Fisher, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.05
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.212, 41.291, 72.154, 90.00, 104.39, 90.00
R / Rfree (%)	12 / 15.1

The binding sites of Zinc atom in the Refine Atomic Structure of Human Carbonic Anhydrase II (pdb code 2ili). 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 Refine Atomic Structure of Human Carbonic Anhydrase II, PDB code: 2ili:

Zinc binding site 1 out of 1 in the Refine Atomic Structure of 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 Refine Atomic Structure of Human Carbonic Anhydrase II within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn262 b:5.3 occ:1.00 O A:HOH1001 1.9 8.5 1.0 NE2 A:HIS94 2.0 5.6 1.0 ND1 A:HIS119 2.0 5.9 1.0 NE2 A:HIS96 2.0 5.8 1.0 CE1 A:HIS119 2.9 5.7 1.0 CD2 A:HIS96 3.0 5.8 1.0 CD2 A:HIS94 3.0 6.0 1.0 CE1 A:HIS94 3.0 5.9 1.0 CE1 A:HIS96 3.0 7.0 1.0 CG A:HIS119 3.1 5.5 1.0 CB A:HIS119 3.6 5.9 1.0 O A:HOH1038 3.7 20.7 1.0 O A:HOH1002 3.8 13.0 1.0 OG1 A:THR199 3.8 6.8 1.0 OE1 A:GLU106 4.0 6.6 1.0 NE2 A:HIS119 4.1 6.2 1.0 ND1 A:HIS96 4.1 7.2 1.0 CG A:HIS96 4.1 5.8 1.0 CG A:HIS94 4.1 6.1 1.0 ND1 A:HIS94 4.2 6.5 1.0 CD2 A:HIS119 4.2 5.9 1.0 O A:HOH1004 4.3 18.1 1.0 CD A:GLU106 4.9 6.1 1.0 CA A:HIS119 5.0 5.5 1.0

S.Z.Fisher, C.M.Maupin, M.Budayova-Spano, L.Govindasamy, C.Tu, M.Agbandje-Mckenna, D.N.Silverman, G.A.Voth, R.Mckenna. Atomic Crystal and Molecular Dynamics Simulation Structures of Human Carbonic Anhydrase II: Insights Into the Proton Transfer Mechanism Biochemistry V. 46 2930 2007.
ISSN: ISSN 0006-2960
PubMed: 17319692
DOI: 10.1021/BI062066Y