Zinc in PDB 3mnk: Human Carbonic Anhydrase II Mutant K170H

All present enzymatic activity of Human Carbonic Anhydrase II Mutant K170H:
4.2.1.1;

The structure of Human Carbonic Anhydrase II Mutant K170H, PDB code: 3mnk was solved by J.F.Domsic, R.Mckenna, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	24.81 / 1.75
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.716, 41.562, 72.772, 90.00, 104.53, 90.00
R / Rfree (%)	15 / 18.6

The structure of Human Carbonic Anhydrase II Mutant K170H also contains other interesting chemical elements:

Sodium

(Na)

1 atom

The binding sites of Zinc atom in the Human Carbonic Anhydrase II Mutant K170H (pdb code 3mnk). 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 Mutant K170H, PDB code: 3mnk:

Zinc binding site 1 out of 1 in the Human Carbonic Anhydrase II Mutant K170H


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 Mutant K170H within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn262 b:9.0 occ:1.00 NE2 A:HIS94 2.0 9.6 1.0 NE2 A:HIS96 2.0 6.5 1.0 ND1 A:HIS119 2.0 6.5 1.0 O A:HOH287 2.1 13.5 1.0 CE1 A:HIS119 2.9 5.1 1.0 CD2 A:HIS96 2.9 7.3 1.0 CD2 A:HIS94 3.0 6.8 1.0 CE1 A:HIS94 3.0 11.4 1.0 CE1 A:HIS96 3.1 10.1 1.0 CG A:HIS119 3.1 6.1 1.0 CB A:HIS119 3.6 4.9 1.0 O A:HOH300 3.8 21.5 1.0 OG1 A:THR199 3.8 9.4 1.0 OE1 A:GLU106 4.0 9.8 1.0 NE2 A:HIS119 4.1 6.8 1.0 CG A:HIS94 4.1 8.5 1.0 CG A:HIS96 4.1 6.9 1.0 ND1 A:HIS94 4.1 10.3 1.0 ND1 A:HIS96 4.1 7.5 1.0 CD2 A:HIS119 4.2 5.7 1.0 O A:HOH302 4.2 20.0 1.0 CD A:GLU106 4.9 11.9 1.0

J.F.Domsic, W.Williams, S.Z.Fisher, C.Tu, M.Agbandje-Mckenna, D.N.Silverman, R.Mckenna. Structural and Kinetic Study of the Extended Active Site For Proton Transfer in Human Carbonic Anhydrase II. Biochemistry V. 49 6394 2010.
ISSN: ISSN 0006-2960
PubMed: 20578724
DOI: 10.1021/BI1007645