Zinc in PDB 6lhn: Rlgsgg-ATPRT6 Ubr Box
Enzymatic activity of Rlgsgg-ATPRT6 Ubr Box
All present enzymatic activity of Rlgsgg-ATPRT6 Ubr Box:
2.3.2.27;
Protein crystallography data
The structure of Rlgsgg-ATPRT6 Ubr Box, PDB code: 6lhn
was solved by
L.Kim,
D.H.Kwon,
H.K.Song,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
38.95 /
2.50
|
Space group
|
P 43 3 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
95.414,
95.414,
95.414,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
21.3 /
25
|
Zinc Binding Sites:
The binding sites of Zinc atom in the Rlgsgg-ATPRT6 Ubr Box
(pdb code 6lhn). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the
Rlgsgg-ATPRT6 Ubr Box, PDB code: 6lhn:
Jump to Zinc binding site number:
1;
2;
3;
Zinc binding site 1 out
of 3 in 6lhn
Go back to
Zinc Binding Sites List in 6lhn
Zinc binding site 1 out
of 3 in the Rlgsgg-ATPRT6 Ubr Box
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Rlgsgg-ATPRT6 Ubr Box within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn201
b:47.2
occ:1.00
|
ND1
|
A:HIS187
|
2.1
|
62.8
|
1.0
|
SG
|
A:CYS172
|
2.3
|
37.6
|
1.0
|
SG
|
A:CYS149
|
2.4
|
34.5
|
1.0
|
SG
|
A:CYS184
|
2.4
|
46.2
|
1.0
|
HB3
|
A:CYS172
|
2.7
|
53.1
|
1.0
|
CE1
|
A:HIS187
|
2.9
|
50.7
|
1.0
|
HE1
|
A:HIS187
|
3.0
|
60.9
|
1.0
|
HB3
|
A:CYS149
|
3.0
|
44.2
|
1.0
|
CB
|
A:CYS172
|
3.0
|
44.2
|
1.0
|
HB2
|
A:HIS187
|
3.1
|
67.7
|
1.0
|
CG
|
A:HIS187
|
3.2
|
46.0
|
1.0
|
CB
|
A:CYS149
|
3.2
|
36.8
|
1.0
|
H
|
A:CYS184
|
3.4
|
61.2
|
1.0
|
HB2
|
A:CYS172
|
3.4
|
53.1
|
1.0
|
HA
|
A:CYS149
|
3.4
|
47.8
|
1.0
|
HB3
|
A:CYS184
|
3.4
|
56.8
|
1.0
|
HB2
|
A:CYS121
|
3.6
|
60.6
|
1.0
|
CB
|
A:CYS184
|
3.6
|
47.3
|
1.0
|
CB
|
A:HIS187
|
3.7
|
56.4
|
1.0
|
CA
|
A:CYS149
|
3.9
|
39.8
|
1.0
|
NE2
|
A:HIS187
|
4.0
|
44.1
|
1.0
|
HB2
|
A:CYS149
|
4.1
|
44.2
|
1.0
|
N
|
A:CYS184
|
4.1
|
51.0
|
1.0
|
CD2
|
A:HIS187
|
4.2
|
53.7
|
1.0
|
HB3
|
A:HIS187
|
4.2
|
67.7
|
1.0
|
ZN
|
A:ZN202
|
4.3
|
45.3
|
1.0
|
HB2
|
A:CYS184
|
4.3
|
56.8
|
1.0
|
CA
|
A:CYS184
|
4.4
|
48.4
|
1.0
|
CA
|
A:CYS172
|
4.4
|
40.6
|
1.0
|
CB
|
A:CYS121
|
4.4
|
50.5
|
1.0
|
HB3
|
A:CYS121
|
4.5
|
60.6
|
1.0
|
C
|
A:CYS172
|
4.6
|
36.8
|
1.0
|
HE2
|
A:HIS187
|
4.8
|
53.0
|
1.0
|
O
|
A:CYS172
|
4.8
|
47.6
|
1.0
|
N
|
A:HIS187
|
4.8
|
52.1
|
1.0
|
HB2
|
A:ASN186
|
4.8
|
62.7
|
1.0
|
HA
|
A:CYS172
|
4.8
|
48.8
|
1.0
|
H
|
A:HIS187
|
4.8
|
62.5
|
1.0
|
HD22
|
A:ASN186
|
4.9
|
83.3
|
1.0
|
CA
|
A:HIS187
|
4.9
|
61.6
|
1.0
|
C
|
A:CYS149
|
4.9
|
40.6
|
1.0
|
N
|
A:CYS149
|
4.9
|
45.5
|
1.0
|
C
|
A:CYS184
|
4.9
|
58.2
|
1.0
|
O
|
A:CYS149
|
4.9
|
39.9
|
1.0
|
|
Zinc binding site 2 out
of 3 in 6lhn
Go back to
Zinc Binding Sites List in 6lhn
Zinc binding site 2 out
of 3 in the Rlgsgg-ATPRT6 Ubr Box
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Rlgsgg-ATPRT6 Ubr Box within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn202
b:45.3
occ:1.00
|
SG
|
A:CYS149
|
2.3
|
34.5
|
1.0
|
SG
|
A:CYS170
|
2.4
|
35.7
|
1.0
|
SG
|
A:CYS121
|
2.4
|
47.2
|
1.0
|
SG
|
A:CYS146
|
2.4
|
46.9
|
1.0
|
H
|
A:CYS146
|
3.0
|
39.1
|
1.0
|
HB2
|
A:CYS149
|
3.1
|
44.2
|
1.0
|
HB3
|
A:CYS121
|
3.1
|
60.6
|
1.0
|
HB3
|
A:CYS170
|
3.1
|
35.8
|
1.0
|
CB
|
A:CYS170
|
3.1
|
29.9
|
1.0
|
HB2
|
A:CYS170
|
3.1
|
35.8
|
1.0
|
CB
|
A:CYS121
|
3.2
|
50.5
|
1.0
|
HB2
|
A:CYS121
|
3.2
|
60.6
|
1.0
|
CB
|
A:CYS149
|
3.3
|
36.8
|
1.0
|
HB3
|
A:CYS146
|
3.4
|
46.1
|
1.0
|
CB
|
A:CYS146
|
3.5
|
38.4
|
1.0
|
HB3
|
A:CYS172
|
3.6
|
53.1
|
1.0
|
HB2
|
A:SER123
|
3.6
|
60.3
|
1.0
|
HB2
|
A:CYS172
|
3.7
|
53.1
|
1.0
|
HG
|
A:SER123
|
3.8
|
86.7
|
1.0
|
N
|
A:CYS146
|
3.8
|
32.5
|
1.0
|
HB3
|
A:CYS149
|
3.8
|
44.2
|
1.0
|
H
|
A:CYS149
|
3.9
|
54.7
|
1.0
|
CB
|
A:CYS172
|
4.1
|
44.2
|
1.0
|
OG
|
A:SER123
|
4.1
|
72.2
|
1.0
|
CA
|
A:CYS146
|
4.2
|
36.2
|
1.0
|
HE1
|
A:HIS187
|
4.2
|
60.9
|
1.0
|
HB
|
A:ILE145
|
4.3
|
46.9
|
1.0
|
H
|
A:CYS172
|
4.3
|
49.7
|
1.0
|
ZN
|
A:ZN201
|
4.3
|
47.2
|
1.0
|
HB2
|
A:CYS146
|
4.3
|
46.1
|
1.0
|
CB
|
A:SER123
|
4.4
|
50.3
|
1.0
|
CA
|
A:CYS149
|
4.5
|
39.8
|
1.0
|
N
|
A:CYS149
|
4.5
|
45.5
|
1.0
|
H
|
A:SER123
|
4.6
|
63.3
|
1.0
|
CA
|
A:CYS170
|
4.6
|
42.2
|
1.0
|
CA
|
A:CYS121
|
4.6
|
54.6
|
1.0
|
HA
|
A:ILE145
|
4.7
|
46.3
|
1.0
|
CE1
|
A:HIS187
|
4.8
|
50.7
|
1.0
|
C
|
A:CYS146
|
4.8
|
36.5
|
1.0
|
O
|
A:CYS146
|
4.8
|
42.0
|
1.0
|
HA
|
A:CYS149
|
4.8
|
47.8
|
1.0
|
HB3
|
A:SER123
|
4.9
|
60.3
|
1.0
|
HA
|
A:CYS170
|
4.9
|
50.7
|
1.0
|
C
|
A:ILE145
|
4.9
|
41.7
|
1.0
|
|
Zinc binding site 3 out
of 3 in 6lhn
Go back to
Zinc Binding Sites List in 6lhn
Zinc binding site 3 out
of 3 in the Rlgsgg-ATPRT6 Ubr Box
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Rlgsgg-ATPRT6 Ubr Box within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn203
b:43.7
occ:1.00
|
ND1
|
A:HIS155
|
2.0
|
33.6
|
1.0
|
ND1
|
A:HIS158
|
2.0
|
57.0
|
1.0
|
SG
|
A:CYS137
|
2.3
|
43.8
|
1.0
|
SG
|
A:CYS134
|
2.4
|
38.9
|
1.0
|
CE1
|
A:HIS155
|
2.8
|
40.3
|
1.0
|
HE1
|
A:HIS155
|
2.9
|
48.4
|
1.0
|
CE1
|
A:HIS158
|
2.9
|
53.7
|
1.0
|
HE1
|
A:HIS158
|
3.1
|
64.5
|
1.0
|
CG
|
A:HIS158
|
3.1
|
53.0
|
1.0
|
CG
|
A:HIS155
|
3.1
|
44.5
|
1.0
|
HB3
|
A:HIS155
|
3.2
|
69.4
|
1.0
|
HB3
|
A:HIS158
|
3.2
|
66.0
|
1.0
|
HB
|
A:THR136
|
3.3
|
50.2
|
1.0
|
H
|
A:CYS137
|
3.3
|
59.5
|
1.0
|
HB2
|
A:HIS158
|
3.4
|
66.0
|
1.0
|
CB
|
A:CYS134
|
3.4
|
46.3
|
1.0
|
HB3
|
A:CYS134
|
3.4
|
55.6
|
1.0
|
CB
|
A:HIS158
|
3.5
|
55.0
|
1.0
|
HB2
|
A:CYS137
|
3.5
|
54.4
|
1.0
|
CB
|
A:CYS137
|
3.5
|
45.3
|
1.0
|
HB2
|
A:CYS134
|
3.6
|
55.6
|
1.0
|
CB
|
A:HIS155
|
3.7
|
57.8
|
1.0
|
HA
|
A:HIS155
|
3.7
|
71.9
|
1.0
|
N
|
A:CYS137
|
3.8
|
49.5
|
1.0
|
NE2
|
A:HIS155
|
4.0
|
40.9
|
1.0
|
NE2
|
A:HIS158
|
4.1
|
49.9
|
1.0
|
CD2
|
A:HIS155
|
4.2
|
41.7
|
1.0
|
CD2
|
A:HIS158
|
4.2
|
41.8
|
1.0
|
CA
|
A:HIS155
|
4.2
|
59.9
|
1.0
|
CB
|
A:THR136
|
4.3
|
41.9
|
1.0
|
HB3
|
A:CYS137
|
4.3
|
54.4
|
1.0
|
HZ2
|
A:TRP178
|
4.3
|
46.6
|
1.0
|
CA
|
A:CYS137
|
4.3
|
47.2
|
1.0
|
H
|
A:THR136
|
4.5
|
56.2
|
1.0
|
HB2
|
A:HIS155
|
4.5
|
69.4
|
1.0
|
O
|
A:ASP154
|
4.7
|
57.9
|
1.0
|
HA3
|
A:GLY182
|
4.7
|
54.6
|
1.0
|
C
|
A:THR136
|
4.7
|
46.2
|
1.0
|
HG21
|
A:THR136
|
4.7
|
47.7
|
1.0
|
HA
|
A:CYS137
|
4.7
|
56.7
|
1.0
|
HE2
|
A:HIS155
|
4.7
|
49.1
|
1.0
|
CA
|
A:CYS134
|
4.8
|
45.5
|
1.0
|
HE2
|
A:HIS158
|
4.8
|
59.9
|
1.0
|
HE1
|
A:PHE150
|
4.8
|
58.6
|
1.0
|
HB3
|
A:TYR160
|
4.8
|
52.2
|
1.0
|
HA2
|
A:GLY182
|
4.9
|
54.6
|
1.0
|
CZ2
|
A:TRP178
|
4.9
|
38.8
|
1.0
|
CA
|
A:THR136
|
4.9
|
35.2
|
1.0
|
CG2
|
A:THR136
|
5.0
|
39.8
|
1.0
|
CA
|
A:HIS158
|
5.0
|
58.4
|
1.0
|
HE1
|
A:TRP178
|
5.0
|
54.7
|
1.0
|
|
Reference:
L.Kim,
D.H.Kwon,
J.Heo,
M.R.Park,
H.K.Song.
Use of the LC3B-Fusion Technique For Biochemical and Structural Studies of Proteins Involved in the N-Degron Pathway. J.Biol.Chem. 2020.
ISSN: ESSN 1083-351X
PubMed: 31919097
DOI: 10.1074/JBC.RA119.010912
Page generated: Tue Oct 29 02:35:26 2024
|