Zinc in PDB 6fe2: Three Dimensional Structure of Human Carbonic Anhydrase IX

All present enzymatic activity of Three Dimensional Structure of Human Carbonic Anhydrase IX:
4.2.1.1;

The structure of Three Dimensional Structure of Human Carbonic Anhydrase IX, PDB code: 6fe2 was solved by J.Leitans, K.Tars, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	31.70 / 1.87
Space group	H 3
Cell size a, b, c (Å), α, β, γ (°)	152.670, 152.670, 170.700, 90.00, 90.00, 120.00
R / Rfree (%)	17.2 / 19.9

The binding sites of Zinc atom in the Three Dimensional Structure of Human Carbonic Anhydrase IX (pdb code 6fe2). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Three Dimensional Structure of Human Carbonic Anhydrase IX, PDB code: 6fe2:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Three Dimensional Structure of Human Carbonic Anhydrase IX


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Three Dimensional Structure of Human Carbonic Anhydrase IX within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:23.1 occ:1.00 NE2 A:HIS94 2.0 20.8 1.0 NE2 A:HIS96 2.1 19.4 1.0 ND1 A:HIS119 2.1 18.0 1.0 O A:HOH418 2.3 33.4 1.0 O A:HOH569 2.4 30.6 1.0 CD2 A:HIS94 3.0 20.8 1.0 CE1 A:HIS119 3.0 18.1 1.0 CE1 A:HIS94 3.0 20.7 1.0 CE1 A:HIS96 3.1 21.7 1.0 CD2 A:HIS96 3.1 19.8 1.0 CG A:HIS119 3.2 18.0 1.0 CB A:HIS119 3.6 17.1 1.0 OG1 A:THR199 3.8 34.2 1.0 OE2 A:GLU106 4.0 24.4 1.0 ND1 A:HIS94 4.1 20.1 1.0 CG A:HIS94 4.1 18.6 1.0 NE2 A:HIS119 4.2 18.3 1.0 ND1 A:HIS96 4.2 20.9 1.0 CG A:HIS96 4.2 19.6 1.0 CD2 A:HIS119 4.3 18.6 1.0 CD A:GLU106 4.8 24.8 1.0 CH2 A:TRP209 4.8 19.3 1.0

Zinc binding site 2 out of 4 in the Three Dimensional Structure of Human Carbonic Anhydrase IX


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Three Dimensional Structure of Human Carbonic Anhydrase IX within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn301 b:27.9 occ:1.00 O B:HOH469 1.9 38.2 1.0 NE2 B:HIS94 2.0 26.6 1.0 ND1 B:HIS119 2.2 20.5 1.0 NE2 B:HIS96 2.2 27.9 1.0 O B:HOH523 2.4 35.4 1.0 CD2 B:HIS94 3.0 29.2 1.0 CE1 B:HIS119 3.0 19.9 1.0 CE1 B:HIS94 3.1 27.5 1.0 CD2 B:HIS96 3.2 25.8 1.0 CE1 B:HIS96 3.2 28.4 1.0 CG B:HIS119 3.2 20.8 1.0 CB B:HIS119 3.7 21.8 1.0 OE2 B:GLU106 3.8 33.1 1.0 OG1 B:THR199 3.9 26.1 1.0 CG B:HIS94 4.1 28.3 1.0 NE2 B:HIS119 4.2 19.0 1.0 ND1 B:HIS94 4.2 27.1 1.0 ND1 B:HIS96 4.3 28.6 1.0 CD2 B:HIS119 4.3 19.3 1.0 CG B:HIS96 4.3 27.6 1.0 O B:HOH560 4.5 65.1 1.0 CH2 B:TRP209 4.8 22.2 1.0 CD B:GLU106 4.8 32.7 1.0 O B:HOH515 5.0 53.1 1.0

Zinc binding site 3 out of 4 in the Three Dimensional Structure of Human Carbonic Anhydrase IX


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Three Dimensional Structure of Human Carbonic Anhydrase IX within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn301 b:33.1 occ:1.00 NE2 C:HIS94 1.8 23.1 1.0 ND1 C:HIS119 2.1 27.5 1.0 NE2 C:HIS96 2.1 34.4 1.0 O C:HOH406 2.4 36.3 1.0 O C:HOH525 2.5 38.0 1.0 CD2 C:HIS94 2.9 27.5 1.0 CE1 C:HIS94 2.9 26.3 1.0 CE1 C:HIS119 3.0 30.5 1.0 CE1 C:HIS96 3.1 35.3 1.0 CD2 C:HIS96 3.1 33.4 1.0 CG C:HIS119 3.2 29.2 1.0 CB C:HIS119 3.5 29.3 1.0 OG1 C:THR199 3.9 34.9 1.0 ND1 C:HIS94 4.0 25.7 1.0 CG C:HIS94 4.0 26.6 1.0 OE2 C:GLU106 4.0 35.4 1.0 NE2 C:HIS119 4.2 28.8 1.0 ND1 C:HIS96 4.2 34.6 1.0 CG C:HIS96 4.3 34.9 1.0 CD2 C:HIS119 4.3 28.9 1.0 CH2 C:TRP209 4.8 27.7 1.0 O C:HOH521 4.9 49.9 1.0 CD C:GLU106 4.9 38.6 1.0 O C:HOH558 4.9 54.0 1.0

Zinc binding site 4 out of 4 in the Three Dimensional Structure of Human Carbonic Anhydrase IX


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Three Dimensional Structure of Human Carbonic Anhydrase IX within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn301 b:27.7 occ:1.00 O D:HOH480 1.8 29.8 1.0 ND1 D:HIS119 2.0 21.7 1.0 NE2 D:HIS94 2.1 27.1 1.0 NE2 D:HIS96 2.2 28.7 1.0 O D:HOH521 2.3 36.5 1.0 CE1 D:HIS119 2.8 24.3 1.0 CD2 D:HIS94 3.0 28.6 1.0 CE1 D:HIS94 3.1 28.4 1.0 CE1 D:HIS96 3.1 29.6 1.0 CD2 D:HIS96 3.1 29.2 1.0 CG D:HIS119 3.2 23.6 1.0 CB D:HIS119 3.7 22.8 1.0 OG1 D:THR199 3.8 38.1 1.0 NE2 D:HIS119 4.0 22.1 1.0 OE2 D:GLU106 4.0 34.4 1.0 CD2 D:HIS119 4.2 23.1 1.0 CG D:HIS94 4.2 28.6 1.0 ND1 D:HIS94 4.2 25.4 1.0 ND1 D:HIS96 4.3 29.9 1.0 CG D:HIS96 4.3 28.6 1.0 CD D:GLU106 4.8 30.8 1.0 CH2 D:TRP209 4.8 22.4 1.0

J.Kazokaite, R.Niemans, V.Dudutiene, H.M.Becker, J.Leitans, A.Zubriene, L.Baranauskiene, G.Gondi, R.Zeidler, J.Matuliene, K.Tars, A.Yaromina, P.Lambin, L.J.Dubois, D.Matulis. Novel Fluorinated Carbonic Anhydrase IX Inhibitors Reduce Hypoxia-Induced Acidification and Clonogenic Survival of Cancer Cells. Oncotarget V. 9 26800 2018.
ISSN: ESSN 1949-2553
PubMed: 29928486
DOI: 10.18632/ONCOTARGET.25508