Zinc in PDB 1kop: Neisseria Gonorrhoeae Carbonic Anhydrase

All present enzymatic activity of Neisseria Gonorrhoeae Carbonic Anhydrase:
4.2.1.1;

The structure of Neisseria Gonorrhoeae Carbonic Anhydrase, PDB code: 1kop was solved by S.Huang, Y.Xue, L.Chirica, S.Lindskog, B.-H.Jonsson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	5.00 / 1.90
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	47.230, 74.940, 62.380, 90.00, 93.87, 90.00
R / Rfree (%)	20.6 / 27.1

The binding sites of Zinc atom in the Neisseria Gonorrhoeae Carbonic Anhydrase (pdb code 1kop). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Neisseria Gonorrhoeae Carbonic Anhydrase, PDB code: 1kop:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Neisseria Gonorrhoeae Carbonic Anhydrase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Neisseria Gonorrhoeae Carbonic Anhydrase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:14.3 occ:1.00 NE2 A:HIS92 2.1 17.0 1.0 ND1 A:HIS111 2.1 8.4 1.0 NE2 A:HIS94 2.1 12.5 1.0 N1 A:AZI305 2.2 20.9 0.6 O A:HOH307 2.2 14.6 0.4 CD2 A:HIS92 2.8 15.6 1.0 CD2 A:HIS94 2.9 10.5 1.0 N2 A:AZI305 3.0 24.0 0.6 CE1 A:HIS111 3.0 8.2 1.0 CG A:HIS111 3.2 10.1 1.0 CE1 A:HIS92 3.3 16.4 1.0 CE1 A:HIS94 3.3 14.2 1.0 CB A:HIS111 3.6 8.4 1.0 OG1 A:THR177 3.9 13.1 1.0 OE1 A:GLU98 3.9 12.9 1.0 N3 A:AZI305 3.9 20.9 0.6 O A:HOH308 4.0 43.6 0.4 CG A:HIS92 4.1 16.2 1.0 CG A:HIS94 4.1 10.9 1.0 NE2 A:HIS111 4.2 9.1 1.0 O A:HOH365 4.2 27.3 1.0 ND1 A:HIS92 4.2 15.2 1.0 CD2 A:HIS111 4.3 9.4 1.0 ND1 A:HIS94 4.3 11.6 1.0 O A:HOH385 4.7 21.4 1.0 CD A:GLU98 4.9 13.7 1.0

Zinc binding site 2 out of 2 in the Neisseria Gonorrhoeae Carbonic Anhydrase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Neisseria Gonorrhoeae Carbonic Anhydrase within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn302 b:14.5 occ:1.00 ND1 B:HIS111 2.1 8.7 1.0 NE2 B:HIS92 2.1 15.2 1.0 NE2 B:HIS94 2.1 10.8 1.0 N1 B:AZI306 2.1 26.1 0.6 O B:HOH309 2.2 24.2 0.4 CD2 B:HIS92 2.9 14.4 1.0 CE1 B:HIS111 2.9 8.1 1.0 CD2 B:HIS94 2.9 12.3 1.0 N2 B:AZI306 3.0 27.6 0.6 CG B:HIS111 3.2 6.7 1.0 CE1 B:HIS92 3.2 15.3 1.0 CE1 B:HIS94 3.2 12.1 1.0 CB B:HIS111 3.6 7.9 1.0 N3 B:AZI306 3.9 25.4 0.6 OG1 B:THR177 3.9 12.3 1.0 OE1 B:GLU98 3.9 14.4 1.0 O B:HOH310 4.0 42.1 0.4 NE2 B:HIS111 4.1 8.5 1.0 CG B:HIS92 4.1 12.3 1.0 CG B:HIS94 4.1 13.9 1.0 CD2 B:HIS111 4.2 8.6 1.0 ND1 B:HIS92 4.2 12.7 1.0 O B:HOH464 4.2 33.8 1.0 ND1 B:HIS94 4.3 12.4 1.0 O B:HOH496 4.5 27.1 1.0 CD B:GLU98 4.9 11.9 1.0

S.Huang, Y.Xue, E.Sauer-Eriksson, L.Chirica, S.Lindskog, B.H.Jonsson. Crystal Structure of Carbonic Anhydrase From Neisseria Gonorrhoeae and Its Complex with the Inhibitor Acetazolamide. J.Mol.Biol. V. 283 301 1998.
ISSN: ISSN 0022-2836
PubMed: 9761692
DOI: 10.1006/JMBI.1998.2077