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Zinc in PDB 8wzy: A Novel Amidohydrolase

Protein crystallography data

The structure of A Novel Amidohydrolase, PDB code: 8wzy was solved by R.Feng, D.Ma, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.20 / 1.87
Space group P 21 2 21
Cell size a, b, c (Å), α, β, γ (°) 179.745, 42.002, 43.557, 90, 90, 90
R / Rfree (%) 21.2 / 26

Zinc Binding Sites:

The binding sites of Zinc atom in the A Novel Amidohydrolase (pdb code 8wzy). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the A Novel Amidohydrolase, PDB code: 8wzy:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 8wzy

Go back to Zinc Binding Sites List in 8wzy
Zinc binding site 1 out of 2 in the A Novel Amidohydrolase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of A Novel Amidohydrolase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn405

b:25.6
occ:1.00
OQ1 A:KCX150 2.1 22.9 1.0
NE2 A:HIS58 2.2 24.2 1.0
NE2 A:HIS56 2.3 22.1 1.0
OD1 A:ASP267 2.3 21.1 1.0
CX A:KCX150 2.9 25.0 1.0
CG A:ASP267 3.1 22.6 1.0
CE1 A:HIS58 3.2 21.3 1.0
CD2 A:HIS56 3.2 22.8 1.0
CD2 A:HIS58 3.2 22.7 1.0
CE1 A:HIS56 3.2 20.4 1.0
OQ2 A:KCX150 3.3 22.4 1.0
OD2 A:ASP267 3.5 24.5 1.0
ZN A:ZN406 3.6 28.9 1.0
O A:HOH603 3.7 36.2 1.0
NZ A:KCX150 4.0 20.4 1.0
ND1 A:HIS58 4.3 24.8 1.0
CB A:ASP267 4.3 19.9 1.0
CG A:HIS58 4.3 21.8 1.0
ND1 A:HIS56 4.3 20.9 1.0
CG A:HIS56 4.4 20.1 1.0
CE1 A:HIS207 4.4 20.0 1.0
CB A:ALA85 4.5 19.6 1.0
NE2 A:HIS207 4.5 20.7 1.0
CA A:ASP267 4.7 20.2 1.0
O A:ALA85 4.8 22.0 1.0

Zinc binding site 2 out of 2 in 8wzy

Go back to Zinc Binding Sites List in 8wzy
Zinc binding site 2 out of 2 in the A Novel Amidohydrolase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of A Novel Amidohydrolase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn406

b:28.9
occ:1.00
OQ2 A:KCX150 2.0 22.4 1.0
NE2 A:HIS207 2.2 20.7 1.0
ND1 A:HIS184 2.3 23.0 1.0
O A:HOH603 2.8 36.2 1.0
CX A:KCX150 3.0 25.0 1.0
CD2 A:HIS207 3.2 25.4 1.0
CE1 A:HIS184 3.2 25.2 1.0
CE1 A:HIS207 3.2 20.0 1.0
OQ1 A:KCX150 3.2 22.9 1.0
CG A:HIS184 3.3 23.8 1.0
CB A:HIS184 3.5 22.9 1.0
ZN A:ZN405 3.6 25.6 1.0
O A:HOH627 4.0 40.1 1.0
CD A:ARG152 4.1 29.9 1.0
NZ A:KCX150 4.2 20.4 1.0
CE1 A:HIS56 4.3 20.4 1.0
ND1 A:HIS207 4.3 19.4 1.0
CG A:HIS207 4.3 18.4 1.0
NE2 A:HIS184 4.3 26.2 1.0
CD2 A:HIS184 4.4 26.4 1.0
NE2 A:HIS56 4.5 22.1 1.0
OD2 A:ASP267 4.5 24.5 1.0
CG A:ARG152 4.6 26.2 1.0
NH1 A:ARG152 4.7 26.1 1.0
CE A:KCX150 4.8 23.0 1.0
CA A:HIS184 4.9 24.9 1.0

Reference:

D.Ma, R.Feng. A Novel Amidohydrolase Catalyzes the Degradation of Polyacrylamide By Klebsiella Sp. Pcx To Be Published.
Page generated: Fri Aug 22 15:21:32 2025

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