Zinc in PDB 3rge: Crystal Structure of the W5H Mutant of Human Carbonic Anhydrase II

All present enzymatic activity of Crystal Structure of the W5H Mutant of Human Carbonic Anhydrase II:
4.2.1.1;

The structure of Crystal Structure of the W5H Mutant of Human Carbonic Anhydrase II, PDB code: 3rge was solved by J.F.Domsic, A.H.Robbins, R.Mckenna, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.76 / 2.10
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.700, 41.510, 72.642, 90.00, 104.32, 90.00
R / Rfree (%)	14.1 / 18.8

The binding sites of Zinc atom in the Crystal Structure of the W5H Mutant of Human Carbonic Anhydrase II (pdb code 3rge). 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 Crystal Structure of the W5H Mutant of Human Carbonic Anhydrase II, PDB code: 3rge:

Zinc binding site 1 out of 1 in the Crystal Structure of the W5H Mutant 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 Crystal Structure of the W5H Mutant of Human Carbonic Anhydrase II within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn262 b:10.2 occ:1.00 NE2 A:HIS94 2.0 11.4 1.0 NE2 A:HIS96 2.0 8.8 1.0 ND1 A:HIS119 2.0 7.4 1.0 O A:HOH263 2.1 9.6 1.0 CE1 A:HIS119 2.9 5.7 1.0 CD2 A:HIS94 2.9 12.9 1.0 CD2 A:HIS96 3.0 6.2 1.0 CE1 A:HIS96 3.1 10.7 1.0 CE1 A:HIS94 3.1 14.3 1.0 CG A:HIS119 3.2 14.2 1.0 CB A:HIS119 3.6 5.6 1.0 O A:HOH275 3.7 19.6 1.0 OG1 A:THR199 3.9 7.0 1.0 OE1 A:GLU106 4.0 7.4 1.0 NE2 A:HIS119 4.1 5.8 1.0 CG A:HIS94 4.1 15.6 1.0 CG A:HIS96 4.2 7.9 1.0 O A:HOH264 4.2 24.0 1.0 ND1 A:HIS94 4.2 17.8 1.0 ND1 A:HIS96 4.2 6.1 1.0 CD2 A:HIS119 4.2 5.8 1.0 O A:HOH276 4.4 29.2 1.0 CD A:GLU106 4.9 8.8 1.0

R.Mikulski, J.F.Domsic, G.Ling, C.Tu, A.H.Robbins, D.N.Silverman, R.Mckenna. Structure and Catalysis By Carbonic Anhydrase II: Role of Active-Site Tryptophan 5. Arch.Biochem.Biophys. V. 516 97 2011.
ISSN: ISSN 0003-9861
PubMed: 22001224
DOI: 10.1016/J.ABB.2011.09.011