Zinc in PDB 8ihq: Cryo-Em Structure of Ochratoxin A-Detoxifying Amidohydrolase ADH3

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>>> Page 1 <<< Page 2, Binding sites: 11 - 16;

Binding sites:

The binding sites of Zinc atom in the Cryo-Em Structure of Ochratoxin A-Detoxifying Amidohydrolase ADH3 (pdb code 8ihq). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 16 binding sites of Zinc where determined in the Cryo-Em Structure of Ochratoxin A-Detoxifying Amidohydrolase ADH3, PDB code: 8ihq:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Zinc binding site 1 out of 16 in the Cryo-Em Structure of Ochratoxin A-Detoxifying Amidohydrolase ADH3


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Cryo-Em Structure of Ochratoxin A-Detoxifying Amidohydrolase ADH3 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn501 b:81.6 occ:1.00 OQ1 A:KCX210 2.1 49.5 1.0 NE2 A:HIS85 2.3 41.5 1.0 NE2 A:HIS83 2.3 33.6 1.0 CE1 A:HIS85 3.0 37.9 1.0 CX A:KCX210 3.0 49.9 1.0 OD1 A:ASP344 3.1 49.2 1.0 CE1 A:HIS83 3.1 36.2 1.0 OQ2 A:KCX210 3.2 50.4 1.0 CD2 A:HIS83 3.3 39.7 1.0 CD2 A:HIS85 3.5 39.3 1.0 CG A:ASP344 3.7 46.4 1.0 ZN A:ZN502 3.8 89.7 1.0 OD2 A:ASP344 3.9 45.3 1.0 NZ A:KCX210 4.1 45.7 1.0 ND1 A:HIS85 4.2 34.1 1.0 ND1 A:HIS83 4.3 40.7 1.0 CG A:HIS83 4.4 35.3 1.0 CG A:HIS85 4.5 43.0 1.0 O A:LEU128 4.7 54.7 1.0 CB A:ASP344 5.0 38.4 1.0

Zinc binding site 2 out of 16 in the Cryo-Em Structure of Ochratoxin A-Detoxifying Amidohydrolase ADH3


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Cryo-Em Structure of Ochratoxin A-Detoxifying Amidohydrolase ADH3 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn502 b:89.7 occ:1.00 ND1 A:HIS251 2.1 49.3 1.0 NE2 A:HIS271 2.3 45.3 1.0 OQ2 A:KCX210 2.7 50.4 1.0 CD2 A:HIS271 3.0 45.8 1.0 CE1 A:HIS251 3.1 40.8 1.0 CG A:HIS251 3.1 44.5 1.0 CB A:HIS251 3.4 37.7 1.0 CE1 A:HIS271 3.5 44.0 1.0 CX A:KCX210 3.6 49.9 1.0 OQ1 A:KCX210 3.7 49.5 1.0 ZN A:ZN501 3.8 81.6 1.0 CE1 A:HIS83 4.0 36.2 1.0 NE2 A:HIS251 4.2 34.0 1.0 CD2 A:HIS251 4.2 37.4 1.0 CG A:HIS271 4.2 48.7 1.0 CA A:HIS251 4.4 38.3 1.0 ND1 A:HIS271 4.4 44.6 1.0 NE2 A:HIS83 4.5 33.6 1.0 CB A:GLU270 4.5 42.5 1.0 OD2 A:ASP344 4.6 45.3 1.0 NZ A:KCX210 4.7 45.7 1.0 NE2 A:HIS163 4.9 50.0 1.0

Zinc binding site 3 out of 16 in the Cryo-Em Structure of Ochratoxin A-Detoxifying Amidohydrolase ADH3


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Cryo-Em Structure of Ochratoxin A-Detoxifying Amidohydrolase ADH3 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn501 b:81.9 occ:1.00 OQ1 B:KCX210 2.1 49.1 1.0 NE2 B:HIS85 2.3 42.1 1.0 NE2 B:HIS83 2.3 34.3 1.0 CE1 B:HIS85 3.0 37.6 1.0 CX B:KCX210 3.0 50.1 1.0 OD1 B:ASP344 3.1 49.9 1.0 CE1 B:HIS83 3.1 37.8 1.0 OQ2 B:KCX210 3.2 50.0 1.0 CD2 B:HIS83 3.3 40.0 1.0 CD2 B:HIS85 3.5 39.2 1.0 CG B:ASP344 3.7 47.3 1.0 ZN B:ZN502 3.8 87.2 1.0 OD2 B:ASP344 3.9 47.4 1.0 NZ B:KCX210 4.1 46.3 1.0 ND1 B:HIS85 4.2 32.9 1.0 ND1 B:HIS83 4.3 41.9 1.0 CG B:HIS83 4.4 36.4 1.0 CG B:HIS85 4.5 42.1 1.0 O B:LEU128 4.7 53.1 1.0 CB B:ASP344 5.0 37.5 1.0

Zinc binding site 4 out of 16 in the Cryo-Em Structure of Ochratoxin A-Detoxifying Amidohydrolase ADH3


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Cryo-Em Structure of Ochratoxin A-Detoxifying Amidohydrolase ADH3 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn502 b:87.2 occ:1.00 ND1 B:HIS251 2.1 49.1 1.0 NE2 B:HIS271 2.3 46.6 1.0 OQ2 B:KCX210 2.7 50.0 1.0 CD2 B:HIS271 3.0 46.8 1.0 CE1 B:HIS251 3.1 40.7 1.0 CG B:HIS251 3.1 44.7 1.0 CB B:HIS251 3.4 38.5 1.0 CE1 B:HIS271 3.4 43.9 1.0 CX B:KCX210 3.5 50.1 1.0 OQ1 B:KCX210 3.6 49.1 1.0 ZN B:ZN501 3.8 81.9 1.0 CE1 B:HIS83 4.1 37.8 1.0 NE2 B:HIS251 4.2 33.6 1.0 CD2 B:HIS251 4.2 37.3 1.0 CG B:HIS271 4.3 48.6 1.0 CA B:HIS251 4.4 39.4 1.0 ND1 B:HIS271 4.4 45.4 1.0 NE2 B:HIS83 4.5 34.3 1.0 CB B:GLU270 4.6 43.1 1.0 OD2 B:ASP344 4.6 47.4 1.0 NZ B:KCX210 4.7 46.3 1.0 NE2 B:HIS163 4.9 48.3 1.0

Zinc binding site 5 out of 16 in the Cryo-Em Structure of Ochratoxin A-Detoxifying Amidohydrolase ADH3


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Cryo-Em Structure of Ochratoxin A-Detoxifying Amidohydrolase ADH3 within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn501 b:80.2 occ:1.00 OQ1 C:KCX210 2.1 51.1 1.0 NE2 C:HIS85 2.3 42.9 1.0 NE2 C:HIS83 2.3 35.0 1.0 CE1 C:HIS85 3.0 37.5 1.0 CX C:KCX210 3.0 50.9 1.0 OD1 C:ASP344 3.1 49.4 1.0 CE1 C:HIS83 3.1 38.0 1.0 OQ2 C:KCX210 3.2 50.9 1.0 CD2 C:HIS83 3.3 39.5 1.0 CD2 C:HIS85 3.5 38.7 1.0 CG C:ASP344 3.7 46.8 1.0 ZN C:ZN502 3.8 89.2 1.0 OD2 C:ASP344 3.9 46.3 1.0 NZ C:KCX210 4.1 46.1 1.0 ND1 C:HIS85 4.2 33.0 1.0 ND1 C:HIS83 4.3 42.3 1.0 CG C:HIS83 4.4 35.9 1.0 CG C:HIS85 4.5 42.3 1.0 O C:LEU128 4.7 53.7 1.0 CB C:ASP344 5.0 37.3 1.0

Zinc binding site 6 out of 16 in the Cryo-Em Structure of Ochratoxin A-Detoxifying Amidohydrolase ADH3


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of Cryo-Em Structure of Ochratoxin A-Detoxifying Amidohydrolase ADH3 within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn502 b:89.2 occ:1.00 ND1 C:HIS251 2.1 48.8 1.0 NE2 C:HIS271 2.3 46.5 1.0 OQ2 C:KCX210 2.7 50.9 1.0 CD2 C:HIS271 3.0 45.5 1.0 CE1 C:HIS251 3.1 41.3 1.0 CG C:HIS251 3.1 45.4 1.0 CE1 C:HIS271 3.4 44.0 1.0 CB C:HIS251 3.4 39.0 1.0 CX C:KCX210 3.5 50.9 1.0 OQ1 C:KCX210 3.6 51.1 1.0 ZN C:ZN501 3.8 80.2 1.0 CE1 C:HIS83 4.1 38.0 1.0 NE2 C:HIS251 4.2 34.1 1.0 CD2 C:HIS251 4.2 38.7 1.0 CG C:HIS271 4.3 48.7 1.0 CA C:HIS251 4.4 40.3 1.0 ND1 C:HIS271 4.4 44.7 1.0 NE2 C:HIS83 4.5 35.0 1.0 CB C:GLU270 4.6 42.8 1.0 OD2 C:ASP344 4.6 46.3 1.0 NZ C:KCX210 4.7 46.1 1.0 NE2 C:HIS163 4.9 49.6 1.0

Zinc binding site 7 out of 16 in the Cryo-Em Structure of Ochratoxin A-Detoxifying Amidohydrolase ADH3


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 7 of Cryo-Em Structure of Ochratoxin A-Detoxifying Amidohydrolase ADH3 within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn501 b:81.7 occ:1.00 OQ1 D:KCX210 2.1 50.5 1.0 NE2 D:HIS85 2.3 42.5 1.0 NE2 D:HIS83 2.3 34.8 1.0 CE1 D:HIS85 3.0 37.2 1.0 CX D:KCX210 3.0 49.8 1.0 OD1 D:ASP344 3.1 50.1 1.0 CE1 D:HIS83 3.1 37.8 1.0 OQ2 D:KCX210 3.2 48.6 1.0 CD2 D:HIS83 3.3 39.0 1.0 CD2 D:HIS85 3.5 39.1 1.0 CG D:ASP344 3.7 47.0 1.0 ZN D:ZN502 3.8 88.0 1.0 OD2 D:ASP344 3.9 45.9 1.0 NZ D:KCX210 4.1 45.0 1.0 ND1 D:HIS85 4.2 32.3 1.0 ND1 D:HIS83 4.3 40.6 1.0 CG D:HIS83 4.4 35.1 1.0 CG D:HIS85 4.5 43.3 1.0 O D:LEU128 4.7 54.5 1.0 CB D:ASP344 5.0 37.8 1.0

Zinc binding site 8 out of 16 in the Cryo-Em Structure of Ochratoxin A-Detoxifying Amidohydrolase ADH3


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 8 of Cryo-Em Structure of Ochratoxin A-Detoxifying Amidohydrolase ADH3 within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn502 b:88.0 occ:1.00 ND1 D:HIS251 2.1 49.0 1.0 NE2 D:HIS271 2.3 45.7 1.0 OQ2 D:KCX210 2.7 48.6 1.0 CD2 D:HIS271 3.0 46.4 1.0 CE1 D:HIS251 3.1 40.9 1.0 CG D:HIS251 3.1 44.1 1.0 CB D:HIS251 3.4 38.7 1.0 CE1 D:HIS271 3.4 43.7 1.0 CX D:KCX210 3.5 49.8 1.0 OQ1 D:KCX210 3.6 50.5 1.0 ZN D:ZN501 3.8 81.7 1.0 CE1 D:HIS83 4.1 37.8 1.0 NE2 D:HIS251 4.2 33.9 1.0 CD2 D:HIS251 4.2 37.1 1.0 CG D:HIS271 4.3 49.2 1.0 CA D:HIS251 4.4 39.8 1.0 ND1 D:HIS271 4.4 44.2 1.0 NE2 D:HIS83 4.5 34.8 1.0 CB D:GLU270 4.6 43.2 1.0 OD2 D:ASP344 4.6 45.9 1.0 NZ D:KCX210 4.7 45.0 1.0 NE2 D:HIS163 4.9 50.2 1.0

Zinc binding site 9 out of 16 in the Cryo-Em Structure of Ochratoxin A-Detoxifying Amidohydrolase ADH3


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 9 of Cryo-Em Structure of Ochratoxin A-Detoxifying Amidohydrolase ADH3 within 5.0Å range: probe atom residue distance (Å) B Occ E:Zn501 b:83.4 occ:1.00 NE2 E:HIS83 2.3 32.2 1.0 NE2 E:HIS85 2.3 37.8 1.0 OD1 E:ASP344 2.8 48.0 1.0 CE1 E:HIS83 3.1 36.0 1.0 OQ1 E:KCX210 3.2 42.3 1.0 CE1 E:HIS85 3.2 36.0 1.0 CD2 E:HIS85 3.3 36.2 1.0 CD2 E:HIS83 3.3 43.1 1.0 CG E:ASP344 3.5 45.5 1.0 OQ2 E:KCX210 3.5 44.1 1.0 OD2 E:ASP344 3.5 41.6 1.0 CX E:KCX210 3.7 48.9 1.0 ZN E:ZN502 3.8 84.8 1.0 ND1 E:HIS83 4.3 42.2 1.0 ND1 E:HIS85 4.4 38.9 1.0 CG E:HIS83 4.4 42.5 1.0 CG E:HIS85 4.4 45.5 1.0 CB E:ASP344 4.7 41.8 1.0 O E:LEU128 4.9 49.8 1.0 NZ E:KCX210 5.0 44.5 1.0 NE2 E:HIS271 5.0 37.7 1.0

Zinc binding site 10 out of 16 in the Cryo-Em Structure of Ochratoxin A-Detoxifying Amidohydrolase ADH3


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 10 of Cryo-Em Structure of Ochratoxin A-Detoxifying Amidohydrolase ADH3 within 5.0Å range: probe atom residue distance (Å) B Occ E:Zn502 b:84.8 occ:1.00 ND1 E:HIS251 2.3 45.7 1.0 NE2 E:HIS271 2.3 37.7 1.0 CE1 E:HIS251 3.1 38.0 1.0 CD2 E:HIS271 3.1 45.6 1.0 OQ1 E:KCX210 3.2 42.3 1.0 CE1 E:HIS271 3.4 29.9 1.0 CG E:HIS251 3.4 40.6 1.0 ZN E:ZN501 3.8 83.4 1.0 CB E:HIS251 3.9 34.1 1.0 CX E:KCX210 4.1 48.9 1.0 CE1 E:HIS83 4.1 36.0 1.0 NE2 E:HIS251 4.3 26.3 1.0 CG E:HIS271 4.3 43.5 1.0 OQ2 E:KCX210 4.4 44.1 1.0 ND1 E:HIS271 4.4 35.5 1.0 OD2 E:ASP344 4.5 41.6 1.0 CD2 E:HIS251 4.5 32.1 1.0 NE2 E:HIS83 4.5 32.2 1.0 NE2 E:HIS163 4.7 39.6 1.0 CB E:GLU270 4.8 37.6 1.0 CA E:HIS251 4.8 32.9 1.0 CD2 E:HIS163 4.9 41.6 1.0

L.Dai, D.Niu, J.W.Huang, X.Li, P.Shen, H.Li, Z.Xie, J.Min, Y.Hu, Y.Yang, R.T.Guo, C.C.Chen. Cryo-Em Structure and Rational Engineering of A Superefficient Ochratoxin A-Detoxifying Amidohydrolase. J Hazard Mater V. 458 31836 2023.
ISSN: ESSN 1873-3336
PubMed: 37331057
DOI: 10.1016/J.JHAZMAT.2023.131836