Zinc in PDB 8j85: Cryo-Em Structure of Ochratoxin A-Detoxifying Amidohydrolase ADH3 Mutant S88E in Complex with Ochratoxin A

The structure of Cryo-Em Structure of Ochratoxin A-Detoxifying Amidohydrolase ADH3 Mutant S88E in Complex with Ochratoxin A also contains other interesting chemical elements:

Chlorine

(Cl)

8 atoms

Pages:

>>> 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 Mutant S88E in Complex with Ochratoxin A (pdb code 8j85). 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 Mutant S88E in Complex with Ochratoxin A, PDB code: 8j85:
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 Mutant S88E in Complex with Ochratoxin A


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 Mutant S88E in Complex with Ochratoxin A within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn501 b:97.1 occ:1.00 OQ2 A:KCX210 1.8 45.8 1.0 NE2 A:HIS85 2.3 35.0 1.0 NE2 A:HIS83 2.3 28.2 1.0 CX A:KCX210 2.9 52.7 1.0 CE1 A:HIS85 3.0 26.4 1.0 CE1 A:HIS83 3.2 39.8 1.0 CD2 A:HIS83 3.3 36.8 1.0 CAA A:97U503 3.4 43.9 1.0 OQ1 A:KCX210 3.4 48.8 1.0 CD2 A:HIS85 3.4 31.3 1.0 ZN A:ZN502 3.5 91.0 1.0 CAF A:97U503 3.6 49.1 1.0 OAX A:97U503 3.6 61.7 1.0 CAN A:97U503 3.6 49.2 1.0 OD1 A:ASN344 3.7 40.1 1.0 CAB A:97U503 3.7 52.8 1.0 ND2 A:ASN344 3.7 35.9 1.0 NZ A:KCX210 3.8 51.0 1.0 CG A:ASN344 3.9 37.7 1.0 OBB A:97U503 4.0 51.3 1.0 CAE A:97U503 4.1 54.5 1.0 CAC A:97U503 4.2 57.0 1.0 ND1 A:HIS85 4.2 36.2 1.0 ND1 A:HIS83 4.4 49.3 1.0 CAD A:97U503 4.4 52.6 1.0 CG A:HIS83 4.4 38.8 1.0 CG A:HIS85 4.5 32.7 1.0 N A:97U503 4.5 52.3 1.0 O A:LEU128 4.7 49.3 1.0 CB A:LEU128 4.7 24.7 1.0 NE2 A:HIS271 4.9 38.5 1.0 CAJ A:97U503 4.9 54.0 1.0

Zinc binding site 2 out of 16 in the Cryo-Em Structure of Ochratoxin A-Detoxifying Amidohydrolase ADH3 Mutant S88E in Complex with Ochratoxin A


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 Mutant S88E in Complex with Ochratoxin A within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn502 b:91.0 occ:1.00 OQ1 A:KCX210 1.8 48.8 1.0 OAX A:97U503 1.8 61.7 1.0 ND1 A:HIS251 2.3 35.1 1.0 NE2 A:HIS271 2.4 38.5 1.0 CX A:KCX210 2.7 52.7 1.0 CAN A:97U503 2.9 49.2 1.0 OQ2 A:KCX210 3.0 45.8 1.0 CD2 A:HIS271 3.3 35.6 1.0 CE1 A:HIS251 3.3 35.2 1.0 CG A:HIS251 3.3 31.4 1.0 CE1 A:HIS271 3.4 38.3 1.0 ZN A:ZN501 3.5 97.1 1.0 CB A:HIS251 3.6 30.1 1.0 CAA A:97U503 3.6 43.9 1.0 CAB A:97U503 3.7 52.8 1.0 NZ A:KCX210 4.0 51.0 1.0 N A:97U503 4.0 52.3 1.0 CE1 A:HIS83 4.0 39.8 1.0 NE2 A:HIS83 4.3 28.2 1.0 CB A:GLU270 4.3 34.5 1.0 CA A:97U503 4.3 52.0 1.0 NE2 A:HIS251 4.4 34.5 1.0 CG A:HIS271 4.4 37.9 1.0 CD2 A:HIS251 4.4 27.9 1.0 ND1 A:HIS271 4.4 39.2 1.0 CE A:KCX210 4.5 39.9 1.0 CA A:HIS251 4.5 27.5 1.0 ND2 A:ASN344 4.6 35.9 1.0 CG A:GLU270 4.7 44.8 1.0 CAF A:97U503 4.8 49.1 1.0 CAC A:97U503 4.9 57.0 1.0 OXT A:97U503 5.0 45.3 1.0

Zinc binding site 3 out of 16 in the Cryo-Em Structure of Ochratoxin A-Detoxifying Amidohydrolase ADH3 Mutant S88E in Complex with Ochratoxin A


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 Mutant S88E in Complex with Ochratoxin A within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn501 b:95.5 occ:1.00 OQ2 B:KCX210 1.8 46.1 1.0 NE2 B:HIS85 2.3 35.2 1.0 NE2 B:HIS83 2.3 28.3 1.0 CX B:KCX210 2.9 53.1 1.0 CE1 B:HIS85 3.0 27.4 1.0 CE1 B:HIS83 3.2 39.5 1.0 CD2 B:HIS83 3.3 36.1 1.0 CAA B:97U503 3.3 45.1 1.0 OQ1 B:KCX210 3.4 49.9 1.0 CD2 B:HIS85 3.4 31.6 1.0 ZN B:ZN502 3.6 92.8 1.0 CAF B:97U503 3.6 49.8 1.0 OAX B:97U503 3.6 60.6 1.0 CAN B:97U503 3.6 49.0 1.0 OD1 B:ASN344 3.7 39.1 1.0 CAB B:97U503 3.7 53.4 1.0 ND2 B:ASN344 3.7 35.5 1.0 NZ B:KCX210 3.8 51.4 1.0 CG B:ASN344 3.9 37.0 1.0 OBB B:97U503 4.0 51.5 1.0 CAE B:97U503 4.1 54.6 1.0 CAC B:97U503 4.2 57.8 1.0 ND1 B:HIS85 4.2 36.2 1.0 ND1 B:HIS83 4.4 49.3 1.0 CAD B:97U503 4.4 53.1 1.0 CG B:HIS83 4.4 39.4 1.0 N B:97U503 4.5 52.4 1.0 CG B:HIS85 4.5 33.0 1.0 O B:LEU128 4.7 50.2 1.0 CB B:LEU128 4.7 24.1 1.0 NE2 B:HIS271 4.9 38.5 1.0 CAJ B:97U503 4.9 53.7 1.0

Zinc binding site 4 out of 16 in the Cryo-Em Structure of Ochratoxin A-Detoxifying Amidohydrolase ADH3 Mutant S88E in Complex with Ochratoxin A


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 Mutant S88E in Complex with Ochratoxin A within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn502 b:92.8 occ:1.00 OAX B:97U503 1.7 60.6 1.0 OQ1 B:KCX210 1.9 49.9 1.0 ND1 B:HIS251 2.3 35.6 1.0 NE2 B:HIS271 2.3 38.5 1.0 CX B:KCX210 2.9 53.1 1.0 CAN B:97U503 2.9 49.0 1.0 OQ2 B:KCX210 3.1 46.1 1.0 CD2 B:HIS271 3.2 36.1 1.0 CE1 B:HIS251 3.2 36.6 1.0 CE1 B:HIS271 3.3 38.2 1.0 CG B:HIS251 3.3 30.8 1.0 ZN B:ZN501 3.6 95.5 1.0 CB B:HIS251 3.6 30.6 1.0 CAA B:97U503 3.6 45.1 1.0 CAB B:97U503 3.7 53.4 1.0 N B:97U503 3.9 52.4 1.0 CE1 B:HIS83 4.0 39.5 1.0 NZ B:KCX210 4.1 51.4 1.0 CA B:97U503 4.2 52.3 1.0 CB B:GLU270 4.3 35.0 1.0 NE2 B:HIS83 4.3 28.3 1.0 NE2 B:HIS251 4.4 34.5 1.0 CG B:HIS271 4.4 38.1 1.0 ND1 B:HIS271 4.4 39.3 1.0 CD2 B:HIS251 4.4 28.0 1.0 ND2 B:ASN344 4.5 35.5 1.0 CE B:KCX210 4.6 39.4 1.0 CA B:HIS251 4.6 27.3 1.0 CG B:GLU270 4.8 43.8 1.0 CAF B:97U503 4.8 49.8 1.0 OXT B:97U503 4.8 45.2 1.0 C B:97U503 4.9 48.6 1.0 CAC B:97U503 5.0 57.8 1.0

Zinc binding site 5 out of 16 in the Cryo-Em Structure of Ochratoxin A-Detoxifying Amidohydrolase ADH3 Mutant S88E in Complex with Ochratoxin A


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 Mutant S88E in Complex with Ochratoxin A within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn501 b:98.1 occ:1.00 OQ2 C:KCX210 1.8 47.0 1.0 NE2 C:HIS85 2.3 35.5 1.0 NE2 C:HIS83 2.3 27.9 1.0 CX C:KCX210 2.9 53.1 1.0 CE1 C:HIS85 3.0 27.4 1.0 CE1 C:HIS83 3.2 39.7 1.0 CD2 C:HIS83 3.3 37.5 1.0 CAA C:97U503 3.3 44.4 1.0 OQ1 C:KCX210 3.4 49.2 1.0 CD2 C:HIS85 3.4 31.2 1.0 CAF C:97U503 3.6 49.3 1.0 ZN C:ZN502 3.6 89.7 1.0 OAX C:97U503 3.6 61.2 1.0 CAN C:97U503 3.6 48.9 1.0 OD1 C:ASN344 3.7 39.8 1.0 CAB C:97U503 3.7 53.1 1.0 ND2 C:ASN344 3.7 35.9 1.0 NZ C:KCX210 3.8 50.9 1.0 CG C:ASN344 3.9 37.8 1.0 OBB C:97U503 4.0 52.3 1.0 CAE C:97U503 4.1 54.6 1.0 CAC C:97U503 4.2 57.5 1.0 ND1 C:HIS85 4.2 36.2 1.0 ND1 C:HIS83 4.4 49.6 1.0 CAD C:97U503 4.4 53.2 1.0 CG C:HIS83 4.4 39.5 1.0 N C:97U503 4.4 52.7 1.0 CG C:HIS85 4.5 32.4 1.0 O C:LEU128 4.7 49.5 1.0 CB C:LEU128 4.7 25.6 1.0 NE2 C:HIS271 4.9 39.6 1.0 CAJ C:97U503 4.9 54.2 1.0

Zinc binding site 6 out of 16 in the Cryo-Em Structure of Ochratoxin A-Detoxifying Amidohydrolase ADH3 Mutant S88E in Complex with Ochratoxin A


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 Mutant S88E in Complex with Ochratoxin A within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn502 b:89.7 occ:1.00 OAX C:97U503 1.7 61.2 1.0 OQ1 C:KCX210 1.8 49.2 1.0 ND1 C:HIS251 2.3 35.4 1.0 NE2 C:HIS271 2.3 39.6 1.0 CX C:KCX210 2.8 53.1 1.0 CAN C:97U503 2.9 48.9 1.0 OQ2 C:KCX210 3.1 47.0 1.0 CD2 C:HIS271 3.2 36.3 1.0 CE1 C:HIS251 3.2 35.8 1.0 CG C:HIS251 3.3 31.4 1.0 CE1 C:HIS271 3.3 38.9 1.0 ZN C:ZN501 3.6 98.1 1.0 CB C:HIS251 3.6 30.3 1.0 CAA C:97U503 3.7 44.4 1.0 CAB C:97U503 3.8 53.1 1.0 N C:97U503 3.9 52.7 1.0 CE1 C:HIS83 4.0 39.7 1.0 NZ C:KCX210 4.0 50.9 1.0 CA C:97U503 4.2 52.4 1.0 CB C:GLU270 4.2 35.0 1.0 NE2 C:HIS83 4.3 27.9 1.0 CG C:HIS271 4.3 38.8 1.0 NE2 C:HIS251 4.4 34.3 1.0 ND1 C:HIS271 4.4 39.0 1.0 CD2 C:HIS251 4.4 28.1 1.0 CA C:HIS251 4.5 27.2 1.0 CE C:KCX210 4.5 39.6 1.0 ND2 C:ASN344 4.5 35.9 1.0 CG C:GLU270 4.7 44.8 1.0 CAF C:97U503 4.9 49.3 1.0 OXT C:97U503 4.9 45.5 1.0 C C:97U503 4.9 49.0 1.0

Zinc binding site 7 out of 16 in the Cryo-Em Structure of Ochratoxin A-Detoxifying Amidohydrolase ADH3 Mutant S88E in Complex with Ochratoxin A


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 Mutant S88E in Complex with Ochratoxin A within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn501 b:97.4 occ:1.00 OQ2 D:KCX210 1.8 47.0 1.0 NE2 D:HIS85 2.3 35.4 1.0 NE2 D:HIS83 2.3 28.0 1.0 CX D:KCX210 2.9 53.7 1.0 CE1 D:HIS85 3.0 27.2 1.0 CE1 D:HIS83 3.2 39.3 1.0 CD2 D:HIS83 3.3 36.3 1.0 CAA D:97U503 3.3 44.4 1.0 OQ1 D:KCX210 3.4 49.9 1.0 CD2 D:HIS85 3.4 31.3 1.0 ZN D:ZN502 3.6 92.2 1.0 CAF D:97U503 3.6 49.3 1.0 OAX D:97U503 3.6 60.7 1.0 CAN D:97U503 3.6 48.7 1.0 OD1 D:ASN344 3.7 40.1 1.0 CAB D:97U503 3.7 52.8 1.0 ND2 D:ASN344 3.7 36.1 1.0 NZ D:KCX210 3.8 51.6 1.0 CG D:ASN344 3.9 37.9 1.0 OBB D:97U503 4.0 51.1 1.0 CAE D:97U503 4.1 54.8 1.0 CAC D:97U503 4.2 57.6 1.0 ND1 D:HIS85 4.2 36.3 1.0 ND1 D:HIS83 4.4 49.2 1.0 CAD D:97U503 4.4 53.4 1.0 CG D:HIS83 4.4 39.1 1.0 N D:97U503 4.4 52.2 1.0 CG D:HIS85 4.5 32.9 1.0 O D:LEU128 4.7 50.1 1.0 CB D:LEU128 4.7 24.1 1.0 NE2 D:HIS271 4.9 38.0 1.0 CAJ D:97U503 4.9 53.9 1.0

Zinc binding site 8 out of 16 in the Cryo-Em Structure of Ochratoxin A-Detoxifying Amidohydrolase ADH3 Mutant S88E in Complex with Ochratoxin A


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 Mutant S88E in Complex with Ochratoxin A within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn502 b:92.2 occ:1.00 OAX D:97U503 1.7 60.7 1.0 OQ1 D:KCX210 1.9 49.9 1.0 ND1 D:HIS251 2.3 35.9 1.0 NE2 D:HIS271 2.3 38.0 1.0 CX D:KCX210 2.9 53.7 1.0 CAN D:97U503 2.9 48.7 1.0 OQ2 D:KCX210 3.1 47.0 1.0 CD2 D:HIS271 3.2 35.1 1.0 CE1 D:HIS251 3.2 36.1 1.0 CG D:HIS251 3.3 32.0 1.0 CE1 D:HIS271 3.3 37.7 1.0 ZN D:ZN501 3.6 97.4 1.0 CB D:HIS251 3.6 30.8 1.0 CAA D:97U503 3.7 44.4 1.0 CAB D:97U503 3.8 52.8 1.0 N D:97U503 3.9 52.2 1.0 CE1 D:HIS83 4.0 39.3 1.0 NZ D:KCX210 4.1 51.6 1.0 CA D:97U503 4.2 52.0 1.0 CB D:GLU270 4.3 35.5 1.0 NE2 D:HIS83 4.3 28.0 1.0 CG D:HIS271 4.3 37.9 1.0 NE2 D:HIS251 4.4 34.0 1.0 ND1 D:HIS271 4.4 39.2 1.0 CD2 D:HIS251 4.4 28.2 1.0 ND2 D:ASN344 4.5 36.1 1.0 CA D:HIS251 4.5 27.5 1.0 CE D:KCX210 4.5 39.4 1.0 CG D:GLU270 4.7 44.9 1.0 CAF D:97U503 4.8 49.3 1.0 OXT D:97U503 4.9 45.3 1.0 C D:97U503 4.9 48.4 1.0

Zinc binding site 9 out of 16 in the Cryo-Em Structure of Ochratoxin A-Detoxifying Amidohydrolase ADH3 Mutant S88E in Complex with Ochratoxin A


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 Mutant S88E in Complex with Ochratoxin A within 5.0Å range: probe atom residue distance (Å) B Occ E:Zn501 b:97.1 occ:1.00 OQ1 E:KCX210 1.8 45.8 1.0 NE2 E:HIS85 2.3 35.0 1.0 NE2 E:HIS83 2.3 28.2 1.0 CX E:KCX210 2.9 52.7 1.0 CE1 E:HIS85 3.0 26.4 1.0 CE1 E:HIS83 3.2 39.8 1.0 CD2 E:HIS83 3.3 36.8 1.0 CAA E:97U503 3.3 43.9 1.0 OQ2 E:KCX210 3.4 48.8 1.0 CD2 E:HIS85 3.4 31.3 1.0 ZN E:ZN502 3.5 91.0 1.0 CAF E:97U503 3.6 49.1 1.0 OAX E:97U503 3.6 61.7 1.0 CAN E:97U503 3.6 49.2 1.0 OD1 E:ASN344 3.7 40.1 1.0 CAB E:97U503 3.7 52.8 1.0 ND2 E:ASN344 3.7 35.9 1.0 NZ E:KCX210 3.8 51.0 1.0 CG E:ASN344 3.9 37.7 1.0 OBB E:97U503 4.0 51.3 1.0 CAE E:97U503 4.1 54.5 1.0 CAC E:97U503 4.2 57.0 1.0 ND1 E:HIS85 4.2 36.2 1.0 ND1 E:HIS83 4.4 49.3 1.0 CAD E:97U503 4.4 52.6 1.0 CG E:HIS83 4.4 38.8 1.0 CG E:HIS85 4.5 32.7 1.0 N E:97U503 4.5 52.3 1.0 O E:LEU128 4.7 49.3 1.0 CB E:LEU128 4.7 24.7 1.0 NE2 E:HIS271 4.9 38.5 1.0 CAJ E:97U503 4.9 54.0 1.0

Zinc binding site 10 out of 16 in the Cryo-Em Structure of Ochratoxin A-Detoxifying Amidohydrolase ADH3 Mutant S88E in Complex with Ochratoxin A


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 Mutant S88E in Complex with Ochratoxin A within 5.0Å range: probe atom residue distance (Å) B Occ E:Zn502 b:91.0 occ:1.00 OQ2 E:KCX210 1.8 48.8 1.0 OAX E:97U503 1.8 61.7 1.0 ND1 E:HIS251 2.3 35.1 1.0 NE2 E:HIS271 2.4 38.5 1.0 CX E:KCX210 2.7 52.7 1.0 CAN E:97U503 2.9 49.2 1.0 OQ1 E:KCX210 3.0 45.8 1.0 CD2 E:HIS271 3.3 35.6 1.0 CE1 E:HIS251 3.3 35.2 1.0 CG E:HIS251 3.3 31.4 1.0 CE1 E:HIS271 3.4 38.3 1.0 ZN E:ZN501 3.5 97.1 1.0 CB E:HIS251 3.6 30.1 1.0 CAA E:97U503 3.6 43.9 1.0 CAB E:97U503 3.7 52.8 1.0 NZ E:KCX210 4.0 51.0 1.0 N E:97U503 4.0 52.3 1.0 CE1 E:HIS83 4.0 39.8 1.0 NE2 E:HIS83 4.3 28.2 1.0 CB E:GLU270 4.3 34.5 1.0 CA E:97U503 4.3 52.0 1.0 NE2 E:HIS251 4.4 34.5 1.0 CG E:HIS271 4.4 37.9 1.0 CD2 E:HIS251 4.4 27.9 1.0 ND1 E:HIS271 4.4 39.2 1.0 CE E:KCX210 4.5 39.9 1.0 CA E:HIS251 4.5 27.5 1.0 ND2 E:ASN344 4.6 35.9 1.0 CG E:GLU270 4.7 44.8 1.0 CAF E:97U503 4.8 49.1 1.0 CAC E:97U503 4.9 57.0 1.0 OXT E:97U503 5.0 45.3 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