Zinc in PDB 4jsa: Benzenesulfonamide Complexed with Hcaii H94D

All present enzymatic activity of Benzenesulfonamide Complexed with Hcaii H94D:
4.2.1.1;

The structure of Benzenesulfonamide Complexed with Hcaii H94D, PDB code: 4jsa 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)	40.73 / 1.50
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.021, 41.389, 72.050, 90.00, 104.23, 90.00
R / Rfree (%)	17.8 / 21.7

The structure of Benzenesulfonamide Complexed with Hcaii H94D also contains other interesting chemical elements:

Mercury

(Hg)

1 atom

The binding sites of Zinc atom in the Benzenesulfonamide Complexed with Hcaii H94D (pdb code 4jsa). 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 Complexed with Hcaii H94D, PDB code: 4jsa:

Zinc binding site 1 out of 1 in the Benzenesulfonamide Complexed with Hcaii H94D


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Benzenesulfonamide Complexed with Hcaii H94D within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:8.5 occ:1.00 OD1 A:ASP94 1.9 9.3 1.0 NP0 A:FB2303 2.0 9.4 1.0 ND1 A:HIS119 2.1 6.7 1.0 NE2 A:HIS96 2.1 6.2 1.0 CG A:ASP94 2.9 9.8 1.0 CE1 A:HIS119 3.0 4.6 1.0 CD2 A:HIS96 3.0 6.1 1.0 CG A:HIS119 3.1 6.6 1.0 S07 A:FB2303 3.1 14.0 1.0 CE1 A:HIS96 3.1 5.5 1.0 O09 A:FB2303 3.2 14.0 1.0 OD2 A:ASP94 3.3 11.6 1.0 CB A:HIS119 3.5 4.7 1.0 O A:HOH401 3.8 13.1 1.0 O A:HOH525 3.9 22.5 1.0 OG1 A:THR199 4.0 5.2 1.0 O08 A:FB2303 4.1 13.6 1.0 NE2 A:HIS119 4.2 4.5 1.0 CG A:HIS96 4.2 5.0 1.0 CD2 A:HIS119 4.2 5.4 1.0 OE1 A:GLU106 4.2 4.6 1.0 ND1 A:HIS96 4.2 5.7 1.0 CB A:ASP94 4.2 7.7 1.0 C04 A:FB2303 4.3 13.1 1.0 O A:ASP94 4.7 6.4 1.0 C A:ASP94 4.8 6.2 1.0 CA A:HIS119 4.9 3.8 1.0 C03 A:FB2303 4.9 16.5 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