Zinc in PDB 4c5y: Crystal Structure of A. Niger Ochratoxinase

All present enzymatic activity of Crystal Structure of A. Niger Ochratoxinase:
3.4.13.9;

The structure of Crystal Structure of A. Niger Ochratoxinase, PDB code: 4c5y was solved by D.Dobritzsch, H.Wang, G.Schneider, S.Yu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	67.44 / 3.00
Space group	P 4 21 2
Cell size a, b, c (Å), α, β, γ (°)	183.240, 183.240, 78.980, 90.00, 90.00, 90.00
R / Rfree (%)	18.801 / 22.583

The binding sites of Zinc atom in the Crystal Structure of A. Niger Ochratoxinase (pdb code 4c5y). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Crystal Structure of A. Niger Ochratoxinase, PDB code: 4c5y:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Crystal Structure of A. Niger Ochratoxinase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of A. Niger Ochratoxinase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn500 b:95.6 occ:0.50 OQ1 A:KCX246 2.0 84.6 1.0 NE2 A:HIS113 2.2 72.1 1.0 NE2 A:HIS111 2.2 55.6 1.0 CE1 A:HIS113 2.7 71.4 1.0 CX A:KCX246 2.7 80.1 1.0 OQ2 A:KCX246 2.8 79.2 1.0 CE1 A:HIS111 2.9 55.5 1.0 ZN A:ZN501 3.0 94.6 0.5 CD2 A:HIS111 3.4 52.0 1.0 OD2 A:ASP378 3.4 67.3 1.0 CD2 A:HIS113 3.5 73.5 1.0 CG A:ASP378 3.7 64.4 1.0 OD1 A:ASP378 3.8 65.0 1.0 NZ A:KCX246 3.9 71.3 1.0 ND1 A:HIS113 4.0 69.4 1.0 ND1 A:HIS111 4.1 52.7 1.0 CG A:HIS111 4.4 49.4 1.0 NE2 A:HIS307 4.4 55.2 1.0 CG A:HIS113 4.4 65.5 1.0 CE1 A:HIS307 4.7 56.7 1.0 CB A:ASP378 4.8 61.7 1.0 ND1 A:HIS287 4.9 53.1 1.0

Zinc binding site 2 out of 4 in the Crystal Structure of A. Niger Ochratoxinase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of A. Niger Ochratoxinase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn501 b:94.6 occ:0.50 OQ2 A:KCX246 2.0 79.2 1.0 NE2 A:HIS307 2.2 55.2 1.0 ND1 A:HIS287 2.2 53.1 1.0 ZN A:ZN500 3.0 95.6 0.5 CE1 A:HIS287 3.0 54.5 1.0 CX A:KCX246 3.1 80.1 1.0 CD2 A:HIS307 3.2 53.8 1.0 CE1 A:HIS307 3.2 56.7 1.0 CG A:HIS287 3.4 47.2 1.0 OQ1 A:KCX246 3.5 84.6 1.0 CE1 A:HIS111 3.5 55.5 1.0 CB A:HIS287 3.8 43.6 1.0 NE2 A:HIS111 4.0 55.6 1.0 NE2 A:HIS287 4.2 52.0 1.0 ND1 A:HIS307 4.3 56.3 1.0 CG A:HIS307 4.3 53.8 1.0 NZ A:KCX246 4.3 71.3 1.0 CD2 A:HIS287 4.4 47.4 1.0 OD2 A:ASP378 4.4 67.3 1.0 NE2 A:HIS191 4.6 62.0 1.0 ND1 A:HIS111 4.7 52.7 1.0 CB A:GLU306 4.8 46.4 1.0 CE A:KCX246 4.8 65.4 1.0 CA A:HIS287 4.9 41.0 1.0 CD2 A:HIS191 5.0 60.6 1.0

Zinc binding site 3 out of 4 in the Crystal Structure of A. Niger Ochratoxinase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of A. Niger Ochratoxinase within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn500 b:0.6 occ:0.50 OQ1 B:KCX246 2.0 83.0 1.0 NE2 B:HIS113 2.2 78.0 1.0 NE2 B:HIS111 2.2 57.8 1.0 CE1 B:HIS113 2.7 77.5 1.0 CX B:KCX246 2.7 81.9 1.0 OQ2 B:KCX246 2.8 80.5 1.0 CE1 B:HIS111 2.9 57.0 1.0 ZN B:ZN501 2.9 0.8 0.5 CD2 B:HIS111 3.4 55.1 1.0 OD2 B:ASP378 3.5 55.4 1.0 CD2 B:HIS113 3.5 79.7 1.0 OD1 B:ASP378 3.7 56.3 1.0 CG B:ASP378 3.8 54.2 1.0 NZ B:KCX246 3.9 75.0 1.0 ND1 B:HIS113 4.0 76.3 1.0 ND1 B:HIS111 4.1 55.8 1.0 CG B:HIS111 4.4 54.1 1.0 NE2 B:HIS307 4.4 58.5 1.0 CG B:HIS113 4.4 73.7 1.0 CE1 B:HIS307 4.8 60.3 1.0 ND1 B:HIS287 4.8 54.0 1.0 CB B:ASP378 4.8 51.8 1.0

Zinc binding site 4 out of 4 in the Crystal Structure of A. Niger Ochratoxinase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structure of A. Niger Ochratoxinase within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn501 b:0.8 occ:0.50 OQ2 B:KCX246 2.0 80.5 1.0 NE2 B:HIS307 2.2 58.5 1.0 ND1 B:HIS287 2.2 54.0 1.0 ZN B:ZN500 2.9 0.6 0.5 CE1 B:HIS287 3.0 57.0 1.0 CX B:KCX246 3.1 81.9 1.0 CD2 B:HIS307 3.1 56.3 1.0 CE1 B:HIS307 3.2 60.3 1.0 CG B:HIS287 3.4 50.6 1.0 OQ1 B:KCX246 3.5 83.0 1.0 CE1 B:HIS111 3.5 57.0 1.0 CB B:HIS287 3.8 45.9 1.0 NE2 B:HIS111 4.0 57.8 1.0 NE2 B:HIS287 4.2 55.3 1.0 ND1 B:HIS307 4.3 57.6 1.0 CG B:HIS307 4.3 53.0 1.0 NZ B:KCX246 4.3 75.0 1.0 CD2 B:HIS287 4.4 51.8 1.0 OD2 B:ASP378 4.5 55.4 1.0 NE2 B:HIS191 4.6 56.8 1.0 ND1 B:HIS111 4.6 55.8 1.0 CB B:GLU306 4.8 45.4 1.0 CA B:HIS287 4.8 42.2 1.0 CE B:KCX246 4.8 68.8 1.0

D.Dobritzsch, H.Wang, G.Schneider, S.Yu. Structural and Functional Characterization of Ochratoxinase, A Novel Mycotoxin Degrading Enzyme. Biochem.J. V. 462 441 2014.
ISSN: ISSN 0264-6021
PubMed: 24947135
DOI: 10.1042/BJ20140382