Zinc in PDB 3dvd: X-Ray Crystal Structure of Mutant N62D of Human Carbonic Anhydrase II

All present enzymatic activity of X-Ray Crystal Structure of Mutant N62D of Human Carbonic Anhydrase II:
4.2.1.1;

The structure of X-Ray Crystal Structure of Mutant N62D of Human Carbonic Anhydrase II, PDB code: 3dvd 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)	21.36 / 1.60
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.772, 41.711, 72.831, 90.00, 104.56, 90.00
R / Rfree (%)	17.9 / 18.3

The binding sites of Zinc atom in the X-Ray Crystal Structure of Mutant N62D of Human Carbonic Anhydrase II (pdb code 3dvd). 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 X-Ray Crystal Structure of Mutant N62D of Human Carbonic Anhydrase II, PDB code: 3dvd:

Zinc binding site 1 out of 1 in the X-Ray Crystal Structure of Mutant N62D 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 X-Ray Crystal Structure of Mutant N62D of Human Carbonic Anhydrase II within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn262 b:9.3 occ:1.00 NE2 A:HIS94 2.1 7.0 1.0 NE2 A:HIS96 2.1 8.2 1.0 O A:HOH1 2.1 30.0 1.0 ND1 A:HIS119 2.1 7.1 1.0 CE1 A:HIS119 2.9 6.0 1.0 CD2 A:HIS96 3.0 10.5 1.0 CD2 A:HIS94 3.0 8.4 1.0 CE1 A:HIS94 3.1 9.7 1.0 CE1 A:HIS96 3.1 9.7 1.0 CG A:HIS119 3.2 5.8 1.0 CB A:HIS119 3.7 6.5 1.0 O A:HOH265 3.7 15.2 1.0 OG1 A:THR199 3.8 9.7 1.0 OE1 A:GLU106 4.0 9.8 1.0 O A:HOH295 4.0 22.6 1.0 NE2 A:HIS119 4.1 7.3 1.0 CG A:HIS96 4.1 6.9 1.0 ND1 A:HIS94 4.1 7.9 1.0 CG A:HIS94 4.2 8.1 1.0 ND1 A:HIS96 4.2 8.5 1.0 CD2 A:HIS119 4.3 7.3 1.0 O A:HOH285 4.7 20.2 1.0 CD A:GLU106 4.9 9.8 1.0

J.Zheng, B.S.Avvaru, C.Tu, R.Mckenna, D.N.Silverman. Role of Hydrophilic Residues in Proton Transfer During Catalysis By Human Carbonic Anhydrase II. Biochemistry V. 47 12028 2008.
ISSN: ISSN 0006-2960
PubMed: 18942852
DOI: 10.1021/BI801473W