Zinc in PDB 4jsz: Benzenesulfonamide Bound to Hcaii H94C

All present enzymatic activity of Benzenesulfonamide Bound to Hcaii H94C:
4.2.1.1;

The structure of Benzenesulfonamide Bound to Hcaii H94C, PDB code: 4jsz was solved by D.P.Martin, Z.S.Hann, S.M.Cohen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.56 / 1.90
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.065, 41.345, 71.959, 90.00, 104.27, 90.00
R / Rfree (%)	16.6 / 23

The binding sites of Zinc atom in the Benzenesulfonamide Bound to Hcaii H94C (pdb code 4jsz). 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 Benzenesulfonamide Bound to Hcaii H94C, PDB code: 4jsz:

Zinc binding site 1 out of 1 in the Benzenesulfonamide Bound to Hcaii H94C


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Benzenesulfonamide Bound to Hcaii H94C within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:8.2 occ:1.00 NP0 A:FB2303 2.0 7.1 1.0 NE2 A:HIS96 2.0 6.0 1.0 ND1 A:HIS119 2.1 4.6 1.0 SG A:CYS94 2.3 7.1 1.0 CE1 A:HIS119 3.0 2.0 1.0 CD2 A:HIS96 3.0 4.5 1.0 CE1 A:HIS96 3.0 6.0 1.0 CG A:HIS119 3.2 2.6 1.0 O09 A:FB2303 3.3 24.1 1.0 S07 A:FB2303 3.3 26.3 1.0 CB A:CYS94 3.5 4.5 1.0 CB A:HIS119 3.6 2.0 1.0 ND1 A:HIS96 4.1 4.7 1.0 NE2 A:HIS119 4.2 2.0 1.0 CG A:HIS96 4.2 4.9 1.0 CD2 A:HIS119 4.2 3.3 1.0 OE1 A:GLU106 4.3 5.0 1.0 O A:CYS94 4.3 4.7 1.0 OG1 A:THR199 4.3 3.1 1.0 C04 A:FB2303 4.4 22.4 1.0 C A:CYS94 4.4 4.9 1.0 O08 A:FB2303 4.4 19.1 1.0 CA A:CYS94 4.5 4.6 1.0 CA A:HIS119 4.9 2.0 1.0 C03 A:FB2303 4.9 26.2 1.0 N A:CYS94 5.0 5.6 1.0 N A:PHE95 5.0 3.4 1.0 N A:HIS119 5.0 2.0 1.0

D.P.Martin, Z.S.Hann, S.M.Cohen. Metalloprotein-Inhibitor Binding: Human Carbonic Anhydrase II As A Model For Probing Metal-Ligand Interactions in A Metalloprotein Active Site. Inorg.Chem. V. 52 12207 2013.
ISSN: ISSN 0020-1669
PubMed: 23706138
DOI: 10.1021/IC400295F