Zinc in PDB 8zg8: Zz-Domain of the Arabidopsis Thaliana E3 Ubiquitin-Protein Ligase PRT1
Enzymatic activity of Zz-Domain of the Arabidopsis Thaliana E3 Ubiquitin-Protein Ligase PRT1
All present enzymatic activity of Zz-Domain of the Arabidopsis Thaliana E3 Ubiquitin-Protein Ligase PRT1:
2.3.2.27;
Protein crystallography data
The structure of Zz-Domain of the Arabidopsis Thaliana E3 Ubiquitin-Protein Ligase PRT1, PDB code: 8zg8
was solved by
W.S.Yang,
H.K.Song,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
48.77 /
1.74
|
Space group
|
P 62 2 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
78.03,
78.03,
70.452,
90,
90,
120
|
R / Rfree (%)
|
23.5 /
27.9
|
Zinc Binding Sites:
The binding sites of Zinc atom in the Zz-Domain of the Arabidopsis Thaliana E3 Ubiquitin-Protein Ligase PRT1
(pdb code 8zg8). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the
Zz-Domain of the Arabidopsis Thaliana E3 Ubiquitin-Protein Ligase PRT1, PDB code: 8zg8:
Jump to Zinc binding site number:
1;
2;
Zinc binding site 1 out
of 2 in 8zg8
Go back to
Zinc Binding Sites List in 8zg8
Zinc binding site 1 out
of 2 in the Zz-Domain of the Arabidopsis Thaliana E3 Ubiquitin-Protein Ligase PRT1
 Mono view
 Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Zz-Domain of the Arabidopsis Thaliana E3 Ubiquitin-Protein Ligase PRT1 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn401
b:32.4
occ:0.79
|
SG
|
A:CYS311
|
2.3
|
28.4
|
1.0
|
SG
|
A:CYS314
|
2.3
|
28.7
|
1.0
|
SG
|
A:CYS338
|
2.3
|
31.1
|
1.0
|
SG
|
A:CYS341
|
2.4
|
32.1
|
1.0
|
HB2
|
A:CYS341
|
2.9
|
42.1
|
1.0
|
H
|
A:CYS314
|
3.0
|
37.2
|
1.0
|
HB3
|
A:CYS314
|
3.1
|
35.1
|
1.0
|
CB
|
A:CYS311
|
3.1
|
24.9
|
1.0
|
HB3
|
A:CYS311
|
3.2
|
29.9
|
1.0
|
HB2
|
A:CYS311
|
3.2
|
29.9
|
1.0
|
H
|
A:CYS338
|
3.2
|
33.9
|
1.0
|
CB
|
A:CYS341
|
3.2
|
35.1
|
1.0
|
CB
|
A:CYS314
|
3.3
|
29.2
|
1.0
|
HB3
|
A:CYS338
|
3.4
|
35.4
|
1.0
|
HB3
|
A:SER313
|
3.4
|
40.5
|
1.0
|
CB
|
A:CYS338
|
3.5
|
29.5
|
1.0
|
H
|
A:CYS341
|
3.7
|
42.8
|
1.0
|
N
|
A:CYS314
|
3.7
|
31.1
|
1.0
|
HG13
|
A:VAL316
|
3.7
|
36.5
|
1.0
|
HB3
|
A:CYS341
|
3.8
|
42.1
|
1.0
|
N
|
A:CYS338
|
4.0
|
28.2
|
1.0
|
CA
|
A:CYS314
|
4.0
|
35.7
|
1.0
|
HB2
|
A:CYS314
|
4.1
|
35.1
|
1.0
|
HG11
|
A:VAL316
|
4.1
|
36.5
|
1.0
|
N
|
A:CYS341
|
4.3
|
35.6
|
1.0
|
HB2
|
A:CYS338
|
4.3
|
35.4
|
1.0
|
CA
|
A:CYS338
|
4.3
|
25.1
|
1.0
|
H
|
A:SER313
|
4.3
|
38.0
|
1.0
|
CA
|
A:CYS341
|
4.4
|
37.9
|
1.0
|
CG1
|
A:VAL316
|
4.4
|
30.4
|
1.0
|
CB
|
A:SER313
|
4.4
|
33.7
|
1.0
|
H
|
A:VAL316
|
4.4
|
36.8
|
1.0
|
H
|
A:GLY315
|
4.5
|
36.6
|
1.0
|
CA
|
A:CYS311
|
4.5
|
22.8
|
1.0
|
HB2
|
A:ASP340
|
4.6
|
46.0
|
1.0
|
HA
|
A:LEU337
|
4.7
|
29.8
|
1.0
|
C
|
A:SER313
|
4.7
|
34.4
|
1.0
|
HB
|
A:VAL316
|
4.7
|
38.4
|
1.0
|
HA
|
A:CYS341
|
4.8
|
45.5
|
1.0
|
C
|
A:CYS314
|
4.8
|
29.4
|
1.0
|
HA
|
A:CYS311
|
4.8
|
27.4
|
1.0
|
HA
|
A:CYS314
|
4.8
|
42.8
|
1.0
|
HD22
|
A:LEU337
|
4.9
|
40.6
|
1.0
|
C
|
A:CYS338
|
4.9
|
29.6
|
1.0
|
N
|
A:GLY315
|
4.9
|
30.5
|
1.0
|
HB2
|
A:SER313
|
4.9
|
40.5
|
1.0
|
O
|
A:CYS338
|
4.9
|
32.5
|
1.0
|
CA
|
A:SER313
|
4.9
|
32.5
|
1.0
|
O
|
A:HOH533
|
5.0
|
39.9
|
1.0
|
N
|
A:SER313
|
5.0
|
31.6
|
1.0
|
|
Zinc binding site 2 out
of 2 in 8zg8
Go back to
Zinc Binding Sites List in 8zg8
Zinc binding site 2 out
of 2 in the Zz-Domain of the Arabidopsis Thaliana E3 Ubiquitin-Protein Ligase PRT1
 Mono view
 Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Zz-Domain of the Arabidopsis Thaliana E3 Ubiquitin-Protein Ligase PRT1 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn402
b:49.5
occ:0.80
|
ND1
|
A:HIS356
|
2.0
|
46.5
|
1.0
|
ND1
|
A:HIS360
|
2.0
|
62.3
|
1.0
|
SG
|
A:CYS329
|
2.3
|
45.9
|
1.0
|
SG
|
A:CYS326
|
2.3
|
45.2
|
1.0
|
H
|
A:CYS329
|
2.7
|
83.5
|
1.0
|
CE1
|
A:HIS356
|
2.8
|
47.5
|
1.0
|
CE1
|
A:HIS360
|
2.9
|
71.1
|
1.0
|
HE1
|
A:HIS356
|
3.0
|
57.0
|
1.0
|
HB3
|
A:HIS360
|
3.0
|
72.0
|
1.0
|
CG
|
A:HIS356
|
3.0
|
47.0
|
1.0
|
CG
|
A:HIS360
|
3.1
|
58.2
|
1.0
|
HE1
|
A:HIS360
|
3.1
|
85.4
|
1.0
|
HB2
|
A:CYS329
|
3.1
|
59.8
|
1.0
|
HA
|
A:HIS356
|
3.1
|
62.8
|
1.0
|
HB2
|
A:HIS356
|
3.2
|
58.6
|
1.0
|
CB
|
A:CYS329
|
3.3
|
49.9
|
1.0
|
CB
|
A:CYS326
|
3.3
|
38.6
|
1.0
|
HB2
|
A:CYS326
|
3.4
|
46.3
|
1.0
|
HB3
|
A:CYS326
|
3.4
|
46.3
|
1.0
|
CB
|
A:HIS360
|
3.4
|
60.0
|
1.0
|
N
|
A:CYS329
|
3.5
|
69.6
|
1.0
|
CB
|
A:HIS356
|
3.5
|
48.9
|
1.0
|
HB2
|
A:ASP328
|
3.5
|
76.7
|
1.0
|
HB3
|
A:TYR335
|
3.6
|
44.3
|
1.0
|
HB2
|
A:HIS360
|
3.6
|
72.0
|
1.0
|
CA
|
A:HIS356
|
3.7
|
52.3
|
1.0
|
CA
|
A:CYS329
|
3.9
|
58.6
|
1.0
|
NE2
|
A:HIS356
|
4.0
|
44.8
|
1.0
|
NE2
|
A:HIS360
|
4.1
|
77.1
|
1.0
|
HB3
|
A:CYS329
|
4.1
|
59.8
|
1.0
|
CD2
|
A:HIS356
|
4.1
|
45.9
|
1.0
|
HB2
|
A:TYR335
|
4.1
|
44.3
|
1.0
|
CD2
|
A:HIS360
|
4.2
|
61.2
|
1.0
|
CB
|
A:TYR335
|
4.2
|
36.9
|
1.0
|
HA
|
A:CYS329
|
4.3
|
70.4
|
1.0
|
HB3
|
A:HIS356
|
4.4
|
58.6
|
1.0
|
H
|
A:ASP328
|
4.4
|
73.3
|
1.0
|
H
|
A:THR357
|
4.5
|
84.3
|
1.0
|
CB
|
A:ASP328
|
4.5
|
63.9
|
1.0
|
C
|
A:ASP328
|
4.6
|
69.7
|
1.0
|
CG
|
A:TYR335
|
4.6
|
36.1
|
1.0
|
N
|
A:HIS356
|
4.7
|
59.6
|
1.0
|
CA
|
A:CYS326
|
4.7
|
32.4
|
1.0
|
HD1
|
A:TYR335
|
4.7
|
43.7
|
1.0
|
HE2
|
A:HIS356
|
4.7
|
53.7
|
1.0
|
C
|
A:HIS356
|
4.8
|
67.4
|
1.0
|
O
|
A:GLN355
|
4.8
|
66.9
|
1.0
|
HE2
|
A:HIS360
|
4.8
|
92.5
|
1.0
|
CA
|
A:ASP328
|
4.9
|
66.5
|
1.0
|
CD1
|
A:TYR335
|
4.9
|
36.4
|
1.0
|
HB3
|
A:ASP328
|
4.9
|
76.7
|
1.0
|
CA
|
A:HIS360
|
4.9
|
68.6
|
1.0
|
HA
|
A:CYS326
|
4.9
|
38.9
|
1.0
|
N
|
A:THR357
|
4.9
|
70.2
|
1.0
|
N
|
A:ASP328
|
4.9
|
61.1
|
1.0
|
HD2
|
A:HIS356
|
5.0
|
55.0
|
1.0
|
|
Reference:
W.S.Yang,
H.K.Song.
Structural Basis For the Recognition of Type-2 N-Degron By PRT1 Plant N-Recognin To Be Published.
Page generated: Fri Aug 22 16:10:22 2025
|