Zinc in PDB 4coq: The Complex of Alpha-Carbonic Anhydrase From Thermovibrio Ammonificans with Inhibitor Sulfanilamide.

All present enzymatic activity of The Complex of Alpha-Carbonic Anhydrase From Thermovibrio Ammonificans with Inhibitor Sulfanilamide.:
4.2.1.1;

The structure of The Complex of Alpha-Carbonic Anhydrase From Thermovibrio Ammonificans with Inhibitor Sulfanilamide., PDB code: 4coq was solved by P.James, M.N.Isupov, C.Sayer, S.Berg, M.Lioliou, H.Kotlar, J.A.Littlechild, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.89 / 1.55
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	83.050, 115.360, 65.540, 90.00, 90.00, 90.00
R / Rfree (%)	17.574 / 20.506

The structure of The Complex of Alpha-Carbonic Anhydrase From Thermovibrio Ammonificans with Inhibitor Sulfanilamide. also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Zinc atom in the The Complex of Alpha-Carbonic Anhydrase From Thermovibrio Ammonificans with Inhibitor Sulfanilamide. (pdb code 4coq). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the The Complex of Alpha-Carbonic Anhydrase From Thermovibrio Ammonificans with Inhibitor Sulfanilamide., PDB code: 4coq:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the The Complex of Alpha-Carbonic Anhydrase From Thermovibrio Ammonificans with Inhibitor Sulfanilamide.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Complex of Alpha-Carbonic Anhydrase From Thermovibrio Ammonificans with Inhibitor Sulfanilamide. within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn299 b:11.4 occ:1.00 O A:HOH2208 1.9 12.4 0.7 ND1 A:HIS131 2.0 5.9 1.0 NE2 A:HIS112 2.1 11.1 1.0 N2 A:SAN300 2.1 10.7 0.3 NE2 A:HIS114 2.1 10.3 1.0 O1 A:SAN300 2.9 14.1 0.3 CE1 A:HIS131 2.9 10.8 1.0 CD2 A:HIS112 3.0 10.2 1.0 S A:SAN300 3.0 9.6 0.3 CE1 A:HIS112 3.1 10.7 1.0 CD2 A:HIS114 3.1 10.4 1.0 CE1 A:HIS114 3.1 11.8 1.0 O A:HOH2210 3.1 21.7 0.7 CG A:HIS131 3.1 9.6 1.0 CB A:HIS131 3.6 9.8 1.0 O A:HOH2209 3.7 17.3 1.0 OE1 A:GLU118 3.8 15.5 1.0 OG1 A:THR198 3.8 12.7 1.0 O2 A:SAN300 4.0 9.2 0.3 NE2 A:HIS131 4.1 11.8 1.0 CG A:HIS112 4.1 9.4 1.0 ND1 A:HIS112 4.1 10.4 1.0 C4 A:SAN300 4.1 12.7 0.3 CD2 A:HIS131 4.2 7.9 1.0 ND1 A:HIS114 4.2 12.0 1.0 CG A:HIS114 4.2 11.3 1.0 O A:HOH2326 4.5 12.4 0.7 O A:HOH2020 4.7 26.7 1.0 CD A:GLU118 4.8 13.7 1.0 C5 A:SAN300 4.9 13.3 0.3 C3 A:SAN300 4.9 13.2 0.3 CA A:HIS131 5.0 10.2 1.0

Zinc binding site 2 out of 2 in the The Complex of Alpha-Carbonic Anhydrase From Thermovibrio Ammonificans with Inhibitor Sulfanilamide.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of The Complex of Alpha-Carbonic Anhydrase From Thermovibrio Ammonificans with Inhibitor Sulfanilamide. within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn299 b:12.8 occ:1.00 O B:HOH2160 2.0 10.1 0.7 ND1 B:HIS131 2.0 9.9 1.0 NE2 B:HIS112 2.0 12.4 1.0 N2 B:SAN300 2.1 11.8 0.3 NE2 B:HIS114 2.1 12.1 1.0 O B:HOH2158 2.3 18.1 0.7 CE1 B:HIS131 2.8 9.3 1.0 CE1 B:HIS114 3.0 13.4 1.0 CD2 B:HIS112 3.0 11.7 1.0 CE1 B:HIS112 3.0 12.9 1.0 CD2 B:HIS114 3.1 13.4 1.0 CG B:HIS131 3.2 9.7 1.0 O1 B:SAN300 3.2 12.6 0.3 S B:SAN300 3.2 12.7 0.3 O B:HOH2161 3.4 15.4 0.3 CB B:HIS131 3.6 9.6 1.0 O B:HOH2159 3.9 22.1 1.0 OG1 B:THR198 3.9 14.8 1.0 OE1 B:GLU118 3.9 15.0 1.0 NE2 B:HIS131 4.0 11.8 1.0 O2 B:SAN300 4.1 11.9 0.3 ND1 B:HIS112 4.1 13.5 1.0 ND1 B:HIS114 4.1 14.0 1.0 CG B:HIS112 4.2 12.1 1.0 CD2 B:HIS131 4.2 13.1 1.0 CG B:HIS114 4.2 12.8 1.0 C4 B:SAN300 4.3 16.8 0.3 O B:HOH2247 4.7 9.9 0.7 O B:HOH2021 4.7 29.0 1.0 CD B:GLU118 4.8 15.2 1.0 C5 B:SAN300 5.0 18.1 0.3

P.James, M.N.Isupov, C.Sayer, V.Saneei, S.Berg, M.Lioliou, H.Kotlar, J.Littlechild. The Structure of A Tetrameric [Alpha]-Carbonic Anhydrase From Thermovibrio Ammonificans Reveals A Core Formed Around Intermolecular Disulfides That Contribute to Its Thermostability Acta Crystallogr.,Sect.D V. 70 2607 2014.
ISSN: ISSN 0907-4449
PubMed: 25286845
DOI: 10.1107/S1399004714016526