Zinc in PDB 2fw4: Carbonic Anhydrase Activators. the First X-Ray Crystallographic Study of An Activator of Isoform I, Structure with L-Histidine.

All present enzymatic activity of Carbonic Anhydrase Activators. the First X-Ray Crystallographic Study of An Activator of Isoform I, Structure with L-Histidine.:
4.2.1.1;

The structure of Carbonic Anhydrase Activators. the First X-Ray Crystallographic Study of An Activator of Isoform I, Structure with L-Histidine., PDB code: 2fw4 was solved by C.Temperini, A.Scozzafava, C.T.Supuran, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	15.00 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	62.138, 70.182, 120.573, 90.00, 90.00, 90.00
R / Rfree (%)	21.3 / 30.3

The binding sites of Zinc atom in the Carbonic Anhydrase Activators. the First X-Ray Crystallographic Study of An Activator of Isoform I, Structure with L-Histidine. (pdb code 2fw4). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Carbonic Anhydrase Activators. the First X-Ray Crystallographic Study of An Activator of Isoform I, Structure with L-Histidine., PDB code: 2fw4:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Carbonic Anhydrase Activators. the First X-Ray Crystallographic Study of An Activator of Isoform I, Structure with L-Histidine.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Carbonic Anhydrase Activators. the First X-Ray Crystallographic Study of An Activator of Isoform I, Structure with L-Histidine. within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn561 b:13.4 occ:1.00 ND1 A:HIS119 2.0 9.2 1.0 NE2 A:HIS94 2.1 11.5 1.0 O A:HOH562 2.3 4.1 1.0 NE2 A:HIS96 2.3 8.6 1.0 CE1 A:HIS119 2.8 8.6 1.0 CE1 A:HIS94 2.9 11.1 1.0 CD2 A:HIS96 3.0 9.2 1.0 CD2 A:HIS94 3.1 9.3 1.0 CG A:HIS119 3.1 8.9 1.0 CE1 A:HIS96 3.5 7.8 1.0 CB A:HIS119 3.6 7.7 1.0 OG1 A:THR199 3.9 7.3 1.0 NE2 A:HIS119 4.0 9.4 1.0 ND1 A:HIS94 4.1 10.2 1.0 OE1 A:GLU106 4.2 12.6 1.0 CD2 A:HIS119 4.2 5.3 1.0 CG A:HIS94 4.2 8.5 1.0 CG A:HIS96 4.3 6.8 1.0 ND1 A:HIS96 4.5 5.8 1.0 O A:HIS500 4.8 50.5 1.0 O A:HOH566 4.9 10.6 1.0 O A:HOH568 4.9 5.6 1.0 CD2 A:HIS200 4.9 11.4 1.0 CH2 A:TRP209 5.0 9.2 1.0

Zinc binding site 2 out of 2 in the Carbonic Anhydrase Activators. the First X-Ray Crystallographic Study of An Activator of Isoform I, Structure with L-Histidine.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Carbonic Anhydrase Activators. the First X-Ray Crystallographic Study of An Activator of Isoform I, Structure with L-Histidine. within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn562 b:13.3 occ:1.00 NE2 B:HIS96 2.0 8.9 1.0 NE2 B:HIS94 2.1 6.0 1.0 ND1 B:HIS119 2.2 7.7 1.0 O B:HOH563 2.4 4.8 1.0 CE1 B:HIS119 3.0 5.9 1.0 CE1 B:HIS94 3.0 4.5 1.0 CD2 B:HIS96 3.0 8.3 1.0 CE1 B:HIS96 3.0 9.7 1.0 CD2 B:HIS94 3.2 4.0 1.0 CG B:HIS119 3.3 7.2 1.0 CB B:HIS119 3.8 8.7 1.0 OG1 B:THR199 3.8 9.7 1.0 ND1 B:HIS96 4.1 11.4 1.0 ND1 B:HIS94 4.1 5.3 1.0 CG B:HIS96 4.2 9.1 1.0 NE2 B:HIS119 4.2 6.8 1.0 CG B:HIS94 4.3 5.2 1.0 OE1 B:GLU106 4.3 11.0 1.0 CD2 B:HIS119 4.3 6.0 1.0 O B:HOH567 4.6 6.6 1.0 O B:HOH581 4.7 15.0 1.0 CH2 B:TRP209 5.0 9.3 1.0

C.Temperini, A.Scozzafava, C.T.Supuran. Carbonic Anhydrase Activators: the First X-Ray Crystallographic Study of An Adduct of Isoform I. Bioorg.Med.Chem.Lett. V. 16 5152 2006.
ISSN: ISSN 0960-894X
PubMed: 16870440
DOI: 10.1016/J.BMCL.2006.07.021