Zinc in PDB 3tvn: Human Carbonic Anhydrase II Proton Transfer Mutant

All present enzymatic activity of Human Carbonic Anhydrase II Proton Transfer Mutant:
4.2.1.1;

The structure of Human Carbonic Anhydrase II Proton Transfer Mutant, PDB code: 3tvn was solved by R.L.Mikulski, D.M.West, K.H.Sippel, B.S.Avvaru, T.Chingkuang, R.Mckenna, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	26.64 / 1.50
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.005, 41.223, 72.059, 90.00, 104.32, 90.00
R / Rfree (%)	17.6 / 21.1

The binding sites of Zinc atom in the Human Carbonic Anhydrase II Proton Transfer Mutant (pdb code 3tvn). 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 Proton Transfer Mutant, PDB code: 3tvn:

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


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 Proton Transfer Mutant within 5.0Å range: probe atom residue distance (Å) B Occ X:Zn262 b:14.2 occ:1.00 O X:HOH394 2.0 13.4 1.0 NE2 X:HIS96 2.0 12.9 1.0 NE2 X:HIS94 2.0 12.9 1.0 ND1 X:HIS119 2.1 14.2 1.0 CE1 X:HIS119 3.0 12.2 1.0 CE1 X:HIS96 3.0 13.2 1.0 CD2 X:HIS94 3.0 15.9 1.0 CD2 X:HIS96 3.0 13.9 1.0 CE1 X:HIS94 3.1 13.5 1.0 CG X:HIS119 3.2 13.3 1.0 CB X:HIS119 3.6 11.3 1.0 O X:HOH401 3.7 20.1 1.0 OG1 X:THR199 3.8 12.3 1.0 OE1 X:GLU106 3.9 13.5 1.0 O X:HOH402 4.0 19.8 1.0 ND1 X:HIS96 4.1 11.7 1.0 NE2 X:HIS119 4.1 11.6 1.0 CG X:HIS94 4.2 16.6 1.0 ND1 X:HIS94 4.2 15.0 1.0 CG X:HIS96 4.2 11.7 1.0 CD2 X:HIS119 4.3 11.1 1.0 O X:HOH373 4.3 29.2 1.0 O X:HOH537 4.4 31.9 1.0 CD X:GLU106 4.8 12.0 1.0

R.Mikulski, D.West, K.H.Sippel, B.S.Avvaru, M.Aggarwal, C.Tu, R.Mckenna, D.N.Silverman. Water Networks in Fast Proton Transfer During Catalysis By Human Carbonic Anhydrase II. Biochemistry V. 52 125 2013.
ISSN: ISSN 0006-2960
PubMed: 23215152
DOI: 10.1021/BI301099K