Zinc in PDB 8yak: Cryo-Em Structure and Rational Engineering of A Novel Efficient Ochratoxin A-Detoxifying Amidohydrolase

The structure of Cryo-Em Structure and Rational Engineering of A Novel Efficient Ochratoxin A-Detoxifying Amidohydrolase 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 and Rational Engineering of A Novel Efficient Ochratoxin A-Detoxifying Amidohydrolase (pdb code 8yak). 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 and Rational Engineering of A Novel Efficient Ochratoxin A-Detoxifying Amidohydrolase, PDB code: 8yak:
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 and Rational Engineering of A Novel Efficient Ochratoxin A-Detoxifying Amidohydrolase


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 and Rational Engineering of A Novel Efficient Ochratoxin A-Detoxifying Amidohydrolase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn501 b:103.0 occ:1.00 NE2 A:HIS85 2.3 49.6 1.0 NE2 A:HIS83 2.3 40.7 1.0 OQ1 A:KCX210 2.6 54.5 1.0 OQ2 A:KCX210 2.7 50.2 1.0 OD1 A:ASN344 3.0 50.4 1.0 CX A:KCX210 3.0 52.3 1.0 CE1 A:HIS85 3.1 43.5 1.0 CE1 A:HIS83 3.1 40.0 1.0 CAA A:97U503 3.1 58.4 1.0 CAB A:97U503 3.4 55.9 1.0 CD2 A:HIS83 3.4 41.5 1.0 ZN A:ZN502 3.4 90.9 1.0 ND2 A:ASN344 3.4 42.7 1.0 CD2 A:HIS85 3.4 56.4 1.0 CAN A:97U503 3.4 62.0 1.0 CG A:ASN344 3.5 43.8 1.0 CAF A:97U503 3.5 61.0 1.0 HAB A:97U503 3.7 58.2 1.0 N A:97U503 3.9 58.0 1.0 CAC A:97U503 3.9 59.8 1.0 OAX A:97U503 4.0 65.3 1.0 CAE A:97U503 4.0 59.3 1.0 H A:97U503 4.0 58.4 1.0 OBB A:97U503 4.1 60.7 1.0 CAD A:97U503 4.2 62.5 1.0 ND1 A:HIS83 4.2 47.1 1.0 ND1 A:HIS85 4.3 52.3 1.0 NZ A:KCX210 4.3 56.5 1.0 NE2 A:HIS271 4.4 47.4 1.0 CE1 A:HIS271 4.4 51.9 1.0 CG A:HIS83 4.4 42.6 1.0 CG A:HIS85 4.5 53.6 1.0 HAM A:97U503 4.7 58.2 1.0 O A:LEU128 4.7 57.2 1.0 CB A:ASN344 4.8 41.9 1.0 H2 A:97U503 4.9 58.0 1.0 CA A:97U503 4.9 57.0 1.0 CLA A:97U503 4.9 78.8 1.0 CAJ A:97U503 4.9 62.3 1.0 OAK A:97U503 5.0 60.4 1.0 HAG A:97U503 5.0 58.0 1.0

Zinc binding site 2 out of 16 in the Cryo-Em Structure and Rational Engineering of A Novel Efficient Ochratoxin A-Detoxifying Amidohydrolase


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 and Rational Engineering of A Novel Efficient Ochratoxin A-Detoxifying Amidohydrolase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn502 b:90.9 occ:1.00 NE2 A:HIS271 1.9 47.4 1.0 OQ2 A:KCX210 2.1 50.2 1.0 ND1 A:HIS251 2.3 47.5 1.0 OAX A:97U503 2.5 65.3 1.0 CX A:KCX210 2.8 52.3 1.0 CD2 A:HIS271 2.9 48.6 1.0 CE1 A:HIS271 2.9 51.9 1.0 H A:97U503 2.9 58.4 1.0 CAN A:97U503 3.1 62.0 1.0 CE1 A:HIS251 3.2 46.5 1.0 HAM A:97U503 3.2 58.2 1.0 CG A:HIS251 3.3 43.3 1.0 ZN A:ZN501 3.4 103.0 1.0 OQ1 A:KCX210 3.4 54.5 1.0 NZ A:KCX210 3.5 56.5 1.0 HAB A:97U503 3.5 58.2 1.0 N A:97U503 3.6 58.0 1.0 CB A:HIS251 3.6 39.1 1.0 CA A:97U503 3.9 57.0 1.0 CAA A:97U503 3.9 58.4 1.0 ND1 A:HIS271 3.9 47.0 1.0 CG A:HIS271 4.0 48.4 1.0 CE1 A:HIS83 4.0 40.0 1.0 CAB A:97U503 4.0 55.9 1.0 OD1 A:ASN344 4.3 50.4 1.0 NE2 A:HIS251 4.3 45.2 1.0 NE2 A:HIS83 4.4 40.7 1.0 CD2 A:HIS251 4.4 45.1 1.0 C A:97U503 4.4 59.1 1.0 O A:97U503 4.6 64.9 1.0 CA A:HIS251 4.6 37.5 1.0 HD2 A:97U503 4.8 58.4 1.0 CB A:GLU270 4.8 41.1 1.0 CE A:KCX210 4.9 56.0 1.0 NE2 A:HIS163 4.9 42.1 1.0

Zinc binding site 3 out of 16 in the Cryo-Em Structure and Rational Engineering of A Novel Efficient Ochratoxin A-Detoxifying Amidohydrolase


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 and Rational Engineering of A Novel Efficient Ochratoxin A-Detoxifying Amidohydrolase within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn501 b:103.0 occ:1.00 NE2 B:HIS85 2.3 49.6 1.0 NE2 B:HIS83 2.3 40.7 1.0 OQ1 B:KCX210 2.6 54.5 1.0 OQ2 B:KCX210 2.7 50.2 1.0 OD1 B:ASN344 3.0 50.4 1.0 CX B:KCX210 3.0 52.3 1.0 CE1 B:HIS85 3.1 43.5 1.0 CE1 B:HIS83 3.1 40.0 1.0 CAA B:97U503 3.1 58.4 1.0 CAB B:97U503 3.4 55.9 1.0 CD2 B:HIS83 3.4 41.5 1.0 ZN B:ZN502 3.4 90.9 1.0 ND2 B:ASN344 3.4 42.7 1.0 CD2 B:HIS85 3.4 56.4 1.0 CAN B:97U503 3.4 62.0 1.0 CG B:ASN344 3.5 43.8 1.0 CAF B:97U503 3.5 61.0 1.0 HAB B:97U503 3.7 58.2 1.0 N B:97U503 3.9 58.0 1.0 CAC B:97U503 3.9 59.8 1.0 OAX B:97U503 4.0 65.3 1.0 CAE B:97U503 4.0 59.3 1.0 H B:97U503 4.0 58.4 1.0 OBB B:97U503 4.1 60.7 1.0 CAD B:97U503 4.2 62.5 1.0 ND1 B:HIS83 4.2 47.1 1.0 ND1 B:HIS85 4.3 52.3 1.0 NZ B:KCX210 4.3 56.5 1.0 NE2 B:HIS271 4.4 47.4 1.0 CE1 B:HIS271 4.4 51.9 1.0 CG B:HIS83 4.4 42.6 1.0 CG B:HIS85 4.5 53.6 1.0 HAM B:97U503 4.7 58.2 1.0 O B:LEU128 4.7 57.2 1.0 CB B:ASN344 4.8 41.9 1.0 H2 B:97U503 4.9 58.0 1.0 CA B:97U503 4.9 57.0 1.0 CLA B:97U503 4.9 78.8 1.0 CAJ B:97U503 4.9 62.3 1.0 OAK B:97U503 5.0 60.4 1.0 HAG B:97U503 5.0 58.0 1.0

Zinc binding site 4 out of 16 in the Cryo-Em Structure and Rational Engineering of A Novel Efficient Ochratoxin A-Detoxifying Amidohydrolase


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 and Rational Engineering of A Novel Efficient Ochratoxin A-Detoxifying Amidohydrolase within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn502 b:90.9 occ:1.00 NE2 B:HIS271 1.9 47.4 1.0 OQ2 B:KCX210 2.1 50.2 1.0 ND1 B:HIS251 2.3 47.5 1.0 OAX B:97U503 2.5 65.3 1.0 CX B:KCX210 2.8 52.3 1.0 CD2 B:HIS271 2.9 48.6 1.0 CE1 B:HIS271 2.9 51.9 1.0 H B:97U503 2.9 58.4 1.0 CAN B:97U503 3.1 62.0 1.0 CE1 B:HIS251 3.2 46.5 1.0 HAM B:97U503 3.2 58.2 1.0 CG B:HIS251 3.3 43.3 1.0 ZN B:ZN501 3.4 103.0 1.0 OQ1 B:KCX210 3.4 54.5 1.0 NZ B:KCX210 3.5 56.5 1.0 HAB B:97U503 3.5 58.2 1.0 N B:97U503 3.6 58.0 1.0 CB B:HIS251 3.6 39.1 1.0 CA B:97U503 3.9 57.0 1.0 CAA B:97U503 3.9 58.4 1.0 ND1 B:HIS271 3.9 47.0 1.0 CG B:HIS271 4.0 48.4 1.0 CE1 B:HIS83 4.0 40.0 1.0 CAB B:97U503 4.0 55.9 1.0 OD1 B:ASN344 4.3 50.4 1.0 NE2 B:HIS251 4.3 45.2 1.0 NE2 B:HIS83 4.4 40.7 1.0 CD2 B:HIS251 4.4 45.1 1.0 C B:97U503 4.4 59.1 1.0 O B:97U503 4.6 64.9 1.0 CA B:HIS251 4.6 37.5 1.0 HD2 B:97U503 4.8 58.4 1.0 CB B:GLU270 4.8 41.1 1.0 CE B:KCX210 4.9 56.0 1.0 NE2 B:HIS163 4.9 42.1 1.0

Zinc binding site 5 out of 16 in the Cryo-Em Structure and Rational Engineering of A Novel Efficient Ochratoxin A-Detoxifying Amidohydrolase


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 and Rational Engineering of A Novel Efficient Ochratoxin A-Detoxifying Amidohydrolase within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn501 b:103.0 occ:1.00 NE2 C:HIS85 2.3 49.6 1.0 NE2 C:HIS83 2.3 40.7 1.0 OQ1 C:KCX210 2.6 54.5 1.0 OQ2 C:KCX210 2.7 50.2 1.0 OD1 C:ASN344 3.0 50.4 1.0 CX C:KCX210 3.0 52.3 1.0 CE1 C:HIS85 3.1 43.5 1.0 CE1 C:HIS83 3.1 40.0 1.0 CAA C:97U503 3.1 58.4 1.0 CAB C:97U503 3.4 55.9 1.0 CD2 C:HIS83 3.4 41.5 1.0 ZN C:ZN502 3.4 90.9 1.0 ND2 C:ASN344 3.4 42.7 1.0 CD2 C:HIS85 3.4 56.4 1.0 CAN C:97U503 3.4 62.0 1.0 CG C:ASN344 3.5 43.8 1.0 CAF C:97U503 3.5 61.0 1.0 HAB C:97U503 3.7 58.2 1.0 N C:97U503 3.9 58.0 1.0 CAC C:97U503 3.9 59.8 1.0 OAX C:97U503 4.0 65.3 1.0 CAE C:97U503 4.0 59.3 1.0 H C:97U503 4.0 58.4 1.0 OBB C:97U503 4.1 60.7 1.0 CAD C:97U503 4.2 62.5 1.0 ND1 C:HIS83 4.2 47.1 1.0 ND1 C:HIS85 4.3 52.3 1.0 NZ C:KCX210 4.3 56.5 1.0 NE2 C:HIS271 4.4 47.4 1.0 CE1 C:HIS271 4.4 51.9 1.0 CG C:HIS83 4.4 42.6 1.0 CG C:HIS85 4.5 53.6 1.0 HAM C:97U503 4.7 58.2 1.0 O C:LEU128 4.7 57.2 1.0 CB C:ASN344 4.8 41.9 1.0 H2 C:97U503 4.9 58.0 1.0 CA C:97U503 4.9 57.0 1.0 CLA C:97U503 4.9 78.8 1.0 CAJ C:97U503 4.9 62.3 1.0 OAK C:97U503 5.0 60.4 1.0 HAG C:97U503 5.0 58.0 1.0

Zinc binding site 6 out of 16 in the Cryo-Em Structure and Rational Engineering of A Novel Efficient Ochratoxin A-Detoxifying Amidohydrolase


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 and Rational Engineering of A Novel Efficient Ochratoxin A-Detoxifying Amidohydrolase within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn502 b:90.9 occ:1.00 NE2 C:HIS271 1.9 47.4 1.0 OQ2 C:KCX210 2.1 50.2 1.0 ND1 C:HIS251 2.3 47.5 1.0 OAX C:97U503 2.5 65.3 1.0 CX C:KCX210 2.8 52.3 1.0 CD2 C:HIS271 2.9 48.6 1.0 CE1 C:HIS271 2.9 51.9 1.0 H C:97U503 2.9 58.4 1.0 CAN C:97U503 3.1 62.0 1.0 CE1 C:HIS251 3.2 46.5 1.0 HAM C:97U503 3.2 58.2 1.0 CG C:HIS251 3.3 43.3 1.0 ZN C:ZN501 3.4 103.0 1.0 OQ1 C:KCX210 3.4 54.5 1.0 NZ C:KCX210 3.5 56.5 1.0 HAB C:97U503 3.5 58.2 1.0 N C:97U503 3.6 58.0 1.0 CB C:HIS251 3.6 39.1 1.0 CA C:97U503 3.9 57.0 1.0 CAA C:97U503 3.9 58.4 1.0 ND1 C:HIS271 3.9 47.0 1.0 CG C:HIS271 4.0 48.4 1.0 CE1 C:HIS83 4.0 40.0 1.0 CAB C:97U503 4.0 55.9 1.0 OD1 C:ASN344 4.3 50.4 1.0 NE2 C:HIS251 4.3 45.2 1.0 NE2 C:HIS83 4.4 40.7 1.0 CD2 C:HIS251 4.4 45.1 1.0 C C:97U503 4.4 59.1 1.0 O C:97U503 4.6 64.9 1.0 CA C:HIS251 4.6 37.5 1.0 HD2 C:97U503 4.8 58.4 1.0 CB C:GLU270 4.8 41.1 1.0 CE C:KCX210 4.8 56.0 1.0 NE2 C:HIS163 4.9 42.1 1.0

Zinc binding site 7 out of 16 in the Cryo-Em Structure and Rational Engineering of A Novel Efficient Ochratoxin A-Detoxifying Amidohydrolase


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 and Rational Engineering of A Novel Efficient Ochratoxin A-Detoxifying Amidohydrolase within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn501 b:103.0 occ:1.00 NE2 D:HIS85 2.3 49.6 1.0 NE2 D:HIS83 2.3 40.7 1.0 OQ1 D:KCX210 2.6 54.5 1.0 OQ2 D:KCX210 2.7 50.2 1.0 OD1 D:ASN344 3.0 50.4 1.0 CX D:KCX210 3.0 52.3 1.0 CE1 D:HIS85 3.1 43.5 1.0 CE1 D:HIS83 3.1 40.0 1.0 CAA D:97U503 3.1 58.4 1.0 CAB D:97U503 3.4 55.9 1.0 CD2 D:HIS83 3.4 41.5 1.0 ZN D:ZN502 3.4 90.9 1.0 ND2 D:ASN344 3.4 42.7 1.0 CD2 D:HIS85 3.4 56.4 1.0 CAN D:97U503 3.4 62.0 1.0 CG D:ASN344 3.5 43.8 1.0 CAF D:97U503 3.5 61.0 1.0 HAB D:97U503 3.7 58.2 1.0 N D:97U503 3.9 58.0 1.0 CAC D:97U503 3.9 59.8 1.0 OAX D:97U503 4.0 65.3 1.0 CAE D:97U503 4.0 59.3 1.0 H D:97U503 4.0 58.4 1.0 OBB D:97U503 4.1 60.7 1.0 CAD D:97U503 4.2 62.5 1.0 ND1 D:HIS83 4.2 47.1 1.0 ND1 D:HIS85 4.3 52.3 1.0 NZ D:KCX210 4.3 56.5 1.0 NE2 D:HIS271 4.4 47.4 1.0 CE1 D:HIS271 4.4 51.9 1.0 CG D:HIS83 4.4 42.6 1.0 CG D:HIS85 4.5 53.6 1.0 HAM D:97U503 4.7 58.2 1.0 O D:LEU128 4.7 57.2 1.0 CB D:ASN344 4.8 41.9 1.0 H2 D:97U503 4.9 58.0 1.0 CA D:97U503 4.9 57.0 1.0 CLA D:97U503 4.9 78.8 1.0 CAJ D:97U503 4.9 62.3 1.0 OAK D:97U503 5.0 60.4 1.0 HAG D:97U503 5.0 58.0 1.0

Zinc binding site 8 out of 16 in the Cryo-Em Structure and Rational Engineering of A Novel Efficient Ochratoxin A-Detoxifying Amidohydrolase


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 and Rational Engineering of A Novel Efficient Ochratoxin A-Detoxifying Amidohydrolase within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn502 b:90.9 occ:1.00 NE2 D:HIS271 1.9 47.4 1.0 OQ2 D:KCX210 2.1 50.2 1.0 ND1 D:HIS251 2.3 47.5 1.0 OAX D:97U503 2.5 65.3 1.0 CX D:KCX210 2.8 52.3 1.0 CD2 D:HIS271 2.9 48.6 1.0 CE1 D:HIS271 2.9 51.9 1.0 H D:97U503 2.9 58.4 1.0 CAN D:97U503 3.1 62.0 1.0 CE1 D:HIS251 3.2 46.5 1.0 HAM D:97U503 3.2 58.2 1.0 CG D:HIS251 3.3 43.3 1.0 ZN D:ZN501 3.4 103.0 1.0 OQ1 D:KCX210 3.4 54.5 1.0 NZ D:KCX210 3.5 56.5 1.0 HAB D:97U503 3.5 58.2 1.0 N D:97U503 3.6 58.0 1.0 CB D:HIS251 3.6 39.1 1.0 CA D:97U503 3.9 57.0 1.0 CAA D:97U503 3.9 58.4 1.0 ND1 D:HIS271 3.9 47.0 1.0 CG D:HIS271 4.0 48.4 1.0 CE1 D:HIS83 4.0 40.0 1.0 CAB D:97U503 4.0 55.9 1.0 OD1 D:ASN344 4.3 50.4 1.0 NE2 D:HIS251 4.3 45.2 1.0 NE2 D:HIS83 4.4 40.7 1.0 CD2 D:HIS251 4.4 45.1 1.0 C D:97U503 4.4 59.1 1.0 O D:97U503 4.6 64.9 1.0 CA D:HIS251 4.6 37.5 1.0 HD2 D:97U503 4.8 58.4 1.0 CB D:GLU270 4.8 41.1 1.0 CE D:KCX210 4.8 56.0 1.0 NE2 D:HIS163 4.9 42.1 1.0

Zinc binding site 9 out of 16 in the Cryo-Em Structure and Rational Engineering of A Novel Efficient Ochratoxin A-Detoxifying Amidohydrolase


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 and Rational Engineering of A Novel Efficient Ochratoxin A-Detoxifying Amidohydrolase within 5.0Å range: probe atom residue distance (Å) B Occ E:Zn501 b:103.0 occ:1.00 NE2 E:HIS85 2.3 49.6 1.0 NE2 E:HIS83 2.3 40.7 1.0 OQ1 E:KCX210 2.6 54.5 1.0 OQ2 E:KCX210 2.7 50.2 1.0 OD1 E:ASN344 3.0 50.4 1.0 CX E:KCX210 3.0 52.3 1.0 CE1 E:HIS85 3.1 43.5 1.0 CE1 E:HIS83 3.1 40.0 1.0 CAA E:97U503 3.1 58.4 1.0 CAB E:97U503 3.4 55.9 1.0 CD2 E:HIS83 3.4 41.5 1.0 ZN E:ZN502 3.4 90.9 1.0 ND2 E:ASN344 3.4 42.7 1.0 CD2 E:HIS85 3.4 56.4 1.0 CAN E:97U503 3.4 62.0 1.0 CG E:ASN344 3.5 43.8 1.0 CAF E:97U503 3.5 61.0 1.0 HAB E:97U503 3.7 58.2 1.0 N E:97U503 3.9 58.0 1.0 CAC E:97U503 3.9 59.8 1.0 OAX E:97U503 4.0 65.3 1.0 CAE E:97U503 4.0 59.3 1.0 H E:97U503 4.0 58.4 1.0 OBB E:97U503 4.1 60.7 1.0 CAD E:97U503 4.2 62.5 1.0 ND1 E:HIS83 4.2 47.1 1.0 ND1 E:HIS85 4.3 52.3 1.0 NZ E:KCX210 4.3 56.5 1.0 NE2 E:HIS271 4.4 47.4 1.0 CE1 E:HIS271 4.4 51.9 1.0 CG E:HIS83 4.4 42.6 1.0 CG E:HIS85 4.5 53.6 1.0 HAM E:97U503 4.7 58.2 1.0 O E:LEU128 4.7 57.2 1.0 CB E:ASN344 4.8 41.9 1.0 H2 E:97U503 4.9 58.0 1.0 CA E:97U503 4.9 57.0 1.0 CLA E:97U503 4.9 78.8 1.0 CAJ E:97U503 4.9 62.3 1.0 OAK E:97U503 5.0 60.4 1.0 HAG E:97U503 5.0 58.0 1.0

Zinc binding site 10 out of 16 in the Cryo-Em Structure and Rational Engineering of A Novel Efficient Ochratoxin A-Detoxifying Amidohydrolase


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 and Rational Engineering of A Novel Efficient Ochratoxin A-Detoxifying Amidohydrolase within 5.0Å range: probe atom residue distance (Å) B Occ E:Zn502 b:90.9 occ:1.00 NE2 E:HIS271 1.9 47.4 1.0 OQ2 E:KCX210 2.1 50.2 1.0 ND1 E:HIS251 2.3 47.5 1.0 OAX E:97U503 2.5 65.3 1.0 CX E:KCX210 2.8 52.3 1.0 CD2 E:HIS271 2.9 48.6 1.0 CE1 E:HIS271 2.9 51.9 1.0 H E:97U503 2.9 58.4 1.0 CAN E:97U503 3.1 62.0 1.0 CE1 E:HIS251 3.2 46.5 1.0 HAM E:97U503 3.2 58.2 1.0 CG E:HIS251 3.3 43.3 1.0 ZN E:ZN501 3.4 103.0 1.0 OQ1 E:KCX210 3.4 54.5 1.0 NZ E:KCX210 3.5 56.5 1.0 HAB E:97U503 3.5 58.2 1.0 N E:97U503 3.6 58.0 1.0 CB E:HIS251 3.6 39.1 1.0 CA E:97U503 3.9 57.0 1.0 CAA E:97U503 3.9 58.4 1.0 ND1 E:HIS271 3.9 47.0 1.0 CG E:HIS271 4.0 48.4 1.0 CE1 E:HIS83 4.0 40.0 1.0 CAB E:97U503 4.0 55.9 1.0 OD1 E:ASN344 4.3 50.4 1.0 NE2 E:HIS251 4.3 45.2 1.0 NE2 E:HIS83 4.4 40.7 1.0 CD2 E:HIS251 4.4 45.1 1.0 C E:97U503 4.4 59.1 1.0 O E:97U503 4.6 64.9 1.0 CA E:HIS251 4.6 37.5 1.0 HD2 E:97U503 4.8 58.4 1.0 CB E:GLU270 4.8 41.1 1.0 CE E:KCX210 4.8 56.0 1.0 NE2 E:HIS163 4.9 42.1 1.0

Y.Hu, L.Dai, Y.Xu, D.Niu, X.Yang, Z.Xie, P.Shen, X.Li, H.Li, L.Zhang, J.Min, R.T.Guo, C.C.Chen. Functional Characterization and Structural Basis of An Efficient Ochratoxin A-Degrading Amidohydrolase. Int.J.Biol.Macromol. V. 278 34831 2024.
ISSN: ISSN 0141-8130
PubMed: 39163957
DOI: 10.1016/J.IJBIOMAC.2024.134831