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

Other elements in 8yak:

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

Zinc Binding Sites:

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 8yak

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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 8yak

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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 8yak

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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 8yak

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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 8yak

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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 8yak

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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 8yak

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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 8yak

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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 8yak

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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 8yak

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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

Reference:

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
Page generated: Sun Feb 9 00:56:46 2025

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