Zinc in PDB 7q0d: Human Carbonic Anhydrase I in Complex with Methyl 2-(Benzenesulfonyl)- 4-Chloro-5-Sulfamoylbenzoate

All present enzymatic activity of Human Carbonic Anhydrase I in Complex with Methyl 2-(Benzenesulfonyl)- 4-Chloro-5-Sulfamoylbenzoate:
4.2.1.1;

The structure of Human Carbonic Anhydrase I in Complex with Methyl 2-(Benzenesulfonyl)- 4-Chloro-5-Sulfamoylbenzoate, PDB code: 7q0d was solved by V.Paketuryte-Latve, A.Smirnov, E.Manakova, S.Grazulis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	55.16 / 1.24
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	62.039, 73.235, 120.473, 90, 90, 90
R / Rfree (%)	13.1 / 15.8

The structure of Human Carbonic Anhydrase I in Complex with Methyl 2-(Benzenesulfonyl)- 4-Chloro-5-Sulfamoylbenzoate also contains other interesting chemical elements:

Chlorine

(Cl)

4 atoms

The binding sites of Zinc atom in the Human Carbonic Anhydrase I in Complex with Methyl 2-(Benzenesulfonyl)- 4-Chloro-5-Sulfamoylbenzoate (pdb code 7q0d). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Human Carbonic Anhydrase I in Complex with Methyl 2-(Benzenesulfonyl)- 4-Chloro-5-Sulfamoylbenzoate, PDB code: 7q0d:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Human Carbonic Anhydrase I in Complex with Methyl 2-(Benzenesulfonyl)- 4-Chloro-5-Sulfamoylbenzoate


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 I in Complex with Methyl 2-(Benzenesulfonyl)- 4-Chloro-5-Sulfamoylbenzoate within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:7.5 occ:1.00 N10 A:84Z302 1.9 13.1 0.5 N10 A:84Z302 1.9 6.6 0.5 NE2 A:HIS94 2.0 7.3 1.0 NE2 A:HIS96 2.0 7.8 1.0 ND1 A:HIS119 2.0 7.3 1.0 CE1 A:HIS119 2.9 7.3 1.0 CE1 A:HIS94 3.0 8.0 1.0 CD2 A:HIS96 3.0 7.2 1.0 O8 A:84Z302 3.0 13.4 0.5 CD2 A:HIS94 3.0 7.5 1.0 S7 A:84Z302 3.0 11.3 0.5 O8 A:84Z302 3.0 5.7 0.5 S7 A:84Z302 3.1 5.9 0.5 CE1 A:HIS96 3.1 8.2 1.0 CG A:HIS119 3.1 6.3 1.0 CB A:HIS119 3.6 7.1 1.0 OG1 A:THR199 3.9 8.3 1.0 O9 A:84Z302 4.1 12.0 0.5 NE2 A:HIS119 4.1 7.0 1.0 C6 A:84Z302 4.1 8.4 0.5 OE2 A:GLU106 4.1 8.5 1.0 ND1 A:HIS94 4.1 8.2 1.0 O9 A:84Z302 4.1 6.7 0.5 CG A:HIS96 4.2 7.0 1.0 ND1 A:HIS96 4.2 8.0 1.0 C6 A:84Z302 4.2 11.1 0.5 CG A:HIS94 4.2 6.7 1.0 CD2 A:HIS119 4.2 7.2 1.0 C5 A:84Z302 4.4 12.1 0.5 O A:HOH481 4.6 9.7 1.0 O A:HOH656 4.6 15.1 1.0 C1 A:84Z302 4.7 11.0 0.5 CL1 A:84Z302 4.8 10.2 0.5 C5 A:84Z302 4.9 10.5 0.5 CH2 A:TRP209 5.0 8.9 1.0

Zinc binding site 2 out of 2 in the Human Carbonic Anhydrase I in Complex with Methyl 2-(Benzenesulfonyl)- 4-Chloro-5-Sulfamoylbenzoate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Human Carbonic Anhydrase I in Complex with Methyl 2-(Benzenesulfonyl)- 4-Chloro-5-Sulfamoylbenzoate within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn301 b:8.4 occ:1.00 N10 B:84Z302 1.9 10.6 0.5 N10 B:84Z302 1.9 9.9 0.5 NE2 B:HIS94 2.0 7.8 1.0 ND1 B:HIS119 2.0 8.2 1.0 NE2 B:HIS96 2.0 8.1 1.0 CE1 B:HIS119 2.9 8.4 1.0 CD2 B:HIS96 3.0 7.8 1.0 CE1 B:HIS94 3.0 9.9 1.0 CD2 B:HIS94 3.0 8.2 1.0 S7 B:84Z302 3.0 9.5 0.5 O8 B:84Z302 3.0 9.9 0.5 S7 B:84Z302 3.1 9.6 0.5 O8 B:84Z302 3.1 10.6 0.5 CE1 B:HIS96 3.1 8.1 1.0 CG B:HIS119 3.1 8.0 1.0 CB B:HIS119 3.6 8.4 1.0 OG1 B:THR199 3.9 9.9 1.0 OE2 B:GLU106 4.1 9.9 1.0 O9 B:84Z302 4.1 10.0 0.5 NE2 B:HIS119 4.1 8.6 1.0 ND1 B:HIS94 4.1 9.5 1.0 CG B:HIS96 4.2 8.1 1.0 O9 B:84Z302 4.2 10.7 0.5 CG B:HIS94 4.2 7.4 1.0 ND1 B:HIS96 4.2 8.8 1.0 C6 B:84Z302 4.2 8.4 0.5 C6 B:84Z302 4.2 12.2 0.5 CD2 B:HIS119 4.2 8.9 1.0 C5 B:84Z302 4.3 14.5 0.5 O B:HOH450 4.6 9.5 1.0 O B:HOH635 4.7 16.4 1.0 C1 B:84Z302 5.0 8.8 0.5 CL1 B:84Z302 5.0 9.5 0.5

A.Zaksauskas, E.Capkauskaite, V.Paketuryte-Latve, A.Smirnov, J.Leitans, A.Kazaks, E.Dvinskis, L.Stancaitis, A.Mickeviciute, J.Jachno, L.Jezepcikas, V.Linkuviene, A.Sakalauskas, E.Manakova, S.Grazulis, J.Matuliene, K.Tars, D.Matulis. Methyl 2-Halo-4-Substituted-5-Sulfamoyl-Benzoates As High Affinity and Selective Inhibitors of Carbonic Anhydrase IX. Int J Mol Sci V. 23 2021.
ISSN: ESSN 1422-0067
PubMed: 35008553
DOI: 10.3390/IJMS23010130