Zinc in PDB 5ezt: Peracetylated Bovine Carbonic Anhydrase II

All present enzymatic activity of Peracetylated Bovine Carbonic Anhydrase II:
4.2.1.1;

The structure of Peracetylated Bovine Carbonic Anhydrase II, PDB code: 5ezt was solved by G.M.Whitesides, K.Kang, J.-M.Choi, J.M.Fox, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	23.81 / 1.54
Space group	P 2 21 21
Cell size a, b, c (Å), α, β, γ (°)	45.701, 63.309, 93.211, 90.00, 90.00, 90.00
R / Rfree (%)	20.9 / 23.9

The binding sites of Zinc atom in the Peracetylated Bovine Carbonic Anhydrase II (pdb code 5ezt). 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 Peracetylated Bovine Carbonic Anhydrase II, PDB code: 5ezt:

Zinc binding site 1 out of 1 in the Peracetylated Bovine 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 Peracetylated Bovine Carbonic Anhydrase II within 5.0Å range: probe atom residue distance (Å) B Occ X:Zn301 b:17.2 occ:1.00 NE2 X:HIS93 2.0 17.4 1.0 NE2 X:HIS95 2.1 18.1 1.0 ND1 X:HIS118 2.1 14.2 1.0 O X:HOH410 2.1 21.8 1.0 O X:HOH598 2.8 25.5 1.0 CD2 X:HIS95 2.9 14.7 1.0 CE1 X:HIS118 3.0 13.9 1.0 CE1 X:HIS93 3.0 14.3 1.0 CD2 X:HIS93 3.0 13.8 1.0 CE1 X:HIS95 3.2 18.3 1.0 CG X:HIS118 3.2 13.2 1.0 CB X:HIS118 3.6 15.0 1.0 OG1 X:THR197 3.8 15.4 1.0 ND1 X:HIS93 4.1 15.5 1.0 O X:HOH592 4.1 38.4 1.0 NE2 X:HIS118 4.1 13.3 1.0 CG X:HIS95 4.1 14.8 1.0 CG X:HIS93 4.2 15.2 1.0 OE1 X:GLU105 4.2 14.8 1.0 ND1 X:HIS95 4.2 15.4 1.0 CD2 X:HIS118 4.2 12.0 1.0 O X:HOH619 4.8 39.8 1.0 CD X:GLU105 5.0 14.5 1.0 CA X:HIS118 5.0 14.1 1.0

K.Kang, J.M.Choi, J.M.Fox, P.W.Snyder, D.T.Moustakas, G.M.Whitesides. Acetylation of Surface Lysine Groups of A Protein Alters the Organization and Composition of Its Crystal Contacts. J.Phys.Chem.B V. 120 6461 2016.
ISSN: ISSN 1089-5647
PubMed: 27292012
DOI: 10.1021/ACS.JPCB.6B01105