Zinc in PDB 5eh5: Human Carbonic Anhydrase II in Complex with Ligand

All present enzymatic activity of Human Carbonic Anhydrase II in Complex with Ligand:
4.2.1.1;

The structure of Human Carbonic Anhydrase II in Complex with Ligand, PDB code: 5eh5 was solved by B.Ren, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.62 / 1.21
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.010, 41.166, 71.816, 90.00, 104.07, 90.00
R / Rfree (%)	17.1 / 18.7

The binding sites of Zinc atom in the Human Carbonic Anhydrase II in Complex with Ligand (pdb code 5eh5). 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 in Complex with Ligand, PDB code: 5eh5:

Zinc binding site 1 out of 1 in the Human Carbonic Anhydrase II in Complex with Ligand


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 in Complex with Ligand within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:5.1 occ:1.00 N6 A:XCZ303 1.9 5.5 1.0 ND1 A:HIS119 2.0 3.7 1.0 NE2 A:HIS94 2.0 5.9 1.0 NE2 A:HIS96 2.0 6.5 1.0 CE1 A:HIS119 2.9 4.8 1.0 CD2 A:HIS94 3.0 6.6 1.0 S5 A:XCZ303 3.0 5.9 1.0 CD2 A:HIS96 3.0 4.9 1.0 CE1 A:HIS96 3.0 5.8 1.0 CE1 A:HIS94 3.1 5.6 1.0 O8 A:XCZ303 3.1 5.5 1.0 CG A:HIS119 3.1 4.1 1.0 CB A:HIS119 3.6 6.3 1.0 O A:HOH647 3.7 32.1 1.0 OG1 A:THR198 3.9 5.0 1.0 OE1 A:GLU106 4.0 5.0 1.0 NE2 A:HIS119 4.1 5.7 1.0 O7 A:XCZ303 4.1 7.0 1.0 ND1 A:HIS94 4.1 6.5 1.0 C4 A:XCZ303 4.1 8.8 1.0 CG A:HIS94 4.1 6.0 1.0 ND1 A:HIS96 4.1 7.1 1.0 CG A:HIS96 4.2 5.7 1.0 CD2 A:HIS119 4.2 4.8 1.0 N3 A:XCZ303 4.7 7.8 1.0 N9 A:XCZ303 4.9 7.8 1.0 CD A:GLU106 4.9 5.6 1.0

L.A.Woods, O.Dolezal, B.Ren, J.H.Ryan, T.S.Peat, S.A.Poulsen. Native State Mass Spectrometry, Surface Plasmon Resonance, and X-Ray Crystallography Correlate Strongly As A Fragment Screening Combination. J.Med.Chem. V. 59 2192 2016.
ISSN: ISSN 0022-2623
PubMed: 26882437
DOI: 10.1021/ACS.JMEDCHEM.5B01940