Zinc in PDB 1zsc: Carbonic Anhydrase II Mutant E117Q, Holo Form

All present enzymatic activity of Carbonic Anhydrase II Mutant E117Q, Holo Form:
4.2.1.1;

The structure of Carbonic Anhydrase II Mutant E117Q, Holo Form, PDB code: 1zsc was solved by C.A.Lesburg, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 1.80
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.700, 41.700, 73.000, 90.00, 104.60, 90.00
R / Rfree (%)	17.7 / n/a

The binding sites of Zinc atom in the Carbonic Anhydrase II Mutant E117Q, Holo Form (pdb code 1zsc). 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 Carbonic Anhydrase II Mutant E117Q, Holo Form, PDB code: 1zsc:

Zinc binding site 1 out of 1 in the Carbonic Anhydrase II Mutant E117Q, Holo Form


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Carbonic Anhydrase II Mutant E117Q, Holo Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn262 b:17.9 occ:1.00 O A:HOH371 2.0 13.7 1.0 NE2 A:HIS94 2.0 8.0 1.0 NE2 A:HIS96 2.0 6.1 1.0 ND1 A:HIS119 2.1 4.5 1.0 CD2 A:HIS94 2.8 7.7 1.0 CD2 A:HIS96 2.9 6.7 1.0 CE1 A:HIS119 3.0 4.3 1.0 CE1 A:HIS94 3.1 8.5 1.0 CE1 A:HIS96 3.1 7.9 1.0 CG A:HIS119 3.2 4.7 1.0 CB A:HIS119 3.6 4.0 1.0 OG1 A:THR199 3.7 4.1 1.0 O A:HOH372 3.9 31.1 1.0 OE1 A:GLU106 3.9 6.3 1.0 O A:HOH370 4.0 27.6 1.0 CG A:HIS94 4.0 7.9 1.0 CG A:HIS96 4.1 6.8 1.0 NE2 A:HIS119 4.1 5.1 1.0 ND1 A:HIS94 4.1 7.7 1.0 ND1 A:HIS96 4.2 7.6 1.0 CD2 A:HIS119 4.2 4.1 1.0 O A:HOH349 4.2 29.5 1.0 CD A:GLU106 4.9 7.2 1.0

C.C.Huang, C.A.Lesburg, L.L.Kiefer, C.A.Fierke, D.W.Christianson. Reversal of the Hydrogen Bond to Zinc Ligand Histidine-119 Dramatically Diminishes Catalysis and Enhances Metal Equilibration Kinetics in Carbonic Anhydrase II. Biochemistry V. 35 3439 1996.
ISSN: ISSN 0006-2960
PubMed: 8639494
DOI: 10.1021/BI9526692