Zinc in PDB 6box: Structure of the S. Pombe CLR4 Catalytic Domain Bound to Sah
Enzymatic activity of Structure of the S. Pombe CLR4 Catalytic Domain Bound to Sah
All present enzymatic activity of Structure of the S. Pombe CLR4 Catalytic Domain Bound to Sah:
2.1.1.43;
Protein crystallography data
The structure of Structure of the S. Pombe CLR4 Catalytic Domain Bound to Sah, PDB code: 6box
was solved by
M.A.Currie,
D.Moazed,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
|
Resolution Low / High (Å)
|
54.19 /
2.41
|
|
Space group
|
C 1 2 1
|
|
Cell size a, b, c (Å), α, β, γ (°)
|
125.625,
71.255,
87.239,
90.00,
120.37,
90.00
|
|
R / Rfree (%)
|
23.1 /
27.6
|
Zinc Binding Sites:
The binding sites of Zinc atom in the Structure of the S. Pombe CLR4 Catalytic Domain Bound to Sah
(pdb code 6box). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 8 binding sites of Zinc where determined in the
Structure of the S. Pombe CLR4 Catalytic Domain Bound to Sah, PDB code: 6box:
Jump to Zinc binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Zinc binding site 1 out
of 8 in 6box
Go back to
Zinc Binding Sites List in 6box
Zinc binding site 1 out
of 8 in the Structure of the S. Pombe CLR4 Catalytic Domain Bound to Sah
 Mono view
 Stereo pair view
|
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Structure of the S. Pombe CLR4 Catalytic Domain Bound to Sah within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn501
b:49.5
occ:1.00
|
SG
|
A:CYS479
|
2.3
|
38.9
|
1.0
|
|
SG
|
A:CYS484
|
2.4
|
53.3
|
1.0
|
|
SG
|
A:CYS477
|
2.5
|
42.3
|
1.0
|
|
SG
|
A:CYS412
|
2.5
|
54.0
|
1.0
|
|
HB3
|
A:CYS477
|
3.1
|
65.8
|
1.0
|
|
H
|
A:CYS412
|
3.3
|
51.2
|
1.0
|
|
H
|
A:CYS479
|
3.4
|
62.9
|
1.0
|
|
CB
|
A:CYS477
|
3.4
|
54.9
|
1.0
|
|
HB2
|
A:CYS412
|
3.4
|
61.1
|
1.0
|
|
HB2
|
A:CYS484
|
3.6
|
70.1
|
1.0
|
|
HB3
|
A:CYS479
|
3.6
|
59.0
|
1.0
|
|
CB
|
A:CYS484
|
3.6
|
58.4
|
1.0
|
|
CB
|
A:CYS479
|
3.6
|
49.1
|
1.0
|
|
CB
|
A:CYS412
|
3.6
|
51.0
|
1.0
|
|
HA
|
A:CYS484
|
3.6
|
70.1
|
1.0
|
|
HE2
|
A:HIS410
|
3.6
|
55.1
|
1.0
|
|
H
|
A:GLY486
|
3.7
|
77.3
|
1.0
|
|
HD2
|
A:HIS410
|
3.8
|
52.1
|
1.0
|
|
HB2
|
A:CYS477
|
3.9
|
65.8
|
1.0
|
|
N
|
A:CYS412
|
4.0
|
42.7
|
1.0
|
|
CA
|
A:CYS484
|
4.1
|
58.5
|
1.0
|
|
N
|
A:CYS479
|
4.2
|
52.4
|
1.0
|
|
NE2
|
A:HIS410
|
4.2
|
45.9
|
1.0
|
|
CD2
|
A:HIS410
|
4.3
|
43.5
|
1.0
|
|
HB2
|
A:CYS479
|
4.3
|
59.0
|
1.0
|
|
H
|
A:TRP487
|
4.4
|
76.6
|
1.0
|
|
HB3
|
A:CYS412
|
4.4
|
61.1
|
1.0
|
|
HA2
|
A:GLY486
|
4.4
|
73.5
|
1.0
|
|
HA
|
A:SER411
|
4.4
|
44.0
|
1.0
|
|
HB3
|
A:CYS484
|
4.4
|
70.1
|
1.0
|
|
CA
|
A:CYS479
|
4.4
|
53.1
|
1.0
|
|
CA
|
A:CYS412
|
4.4
|
45.6
|
1.0
|
|
N
|
A:GLY486
|
4.5
|
64.5
|
1.0
|
|
O
|
A:CYS479
|
4.5
|
53.5
|
1.0
|
|
HN62
|
A:SAH505
|
4.5
|
49.2
|
1.0
|
|
N
|
A:ARG485
|
4.6
|
60.0
|
1.0
|
|
CA
|
A:CYS477
|
4.6
|
48.9
|
1.0
|
|
C
|
A:CYS477
|
4.7
|
43.6
|
1.0
|
|
C
|
A:CYS484
|
4.7
|
57.6
|
1.0
|
|
HB2
|
A:SER481
|
4.8
|
74.3
|
1.0
|
|
HA
|
A:CYS412
|
4.8
|
54.7
|
1.0
|
|
HD1
|
A:TRP487
|
4.9
|
72.5
|
1.0
|
|
C
|
A:CYS479
|
4.9
|
54.9
|
1.0
|
|
N
|
A:LYS478
|
4.9
|
42.4
|
1.0
|
|
H
|
A:LYS478
|
4.9
|
50.9
|
1.0
|
|
C
|
A:SER411
|
4.9
|
37.2
|
1.0
|
|
CA
|
A:GLY486
|
4.9
|
61.3
|
1.0
|
|
O
|
A:CYS477
|
5.0
|
57.8
|
1.0
|
|
Zinc binding site 2 out
of 8 in 6box
Go back to
Zinc Binding Sites List in 6box
Zinc binding site 2 out
of 8 in the Structure of the S. Pombe CLR4 Catalytic Domain Bound to Sah
 Mono view
 Stereo pair view
|
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Structure of the S. Pombe CLR4 Catalytic Domain Bound to Sah within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn502
b:31.9
occ:1.00
|
SG
|
A:CYS307
|
2.3
|
27.3
|
1.0
|
|
SG
|
A:CYS311
|
2.3
|
36.2
|
1.0
|
|
SG
|
A:CYS278
|
2.3
|
22.4
|
1.0
|
|
SG
|
A:CYS260
|
2.4
|
44.8
|
1.0
|
|
HB3
|
A:CYS260
|
2.8
|
55.1
|
1.0
|
|
HB3
|
A:CYS307
|
2.9
|
40.0
|
1.0
|
|
HA
|
A:CYS307
|
3.0
|
41.0
|
1.0
|
|
CB
|
A:CYS307
|
3.1
|
33.3
|
1.0
|
|
CB
|
A:CYS260
|
3.2
|
45.9
|
1.0
|
|
HB3
|
A:CYS311
|
3.2
|
48.7
|
1.0
|
|
CB
|
A:CYS311
|
3.4
|
40.6
|
1.0
|
|
CA
|
A:CYS307
|
3.5
|
34.2
|
1.0
|
|
ZN
|
A:ZN504
|
3.7
|
44.0
|
1.0
|
|
HB2
|
A:CYS278
|
3.7
|
47.3
|
1.0
|
|
CB
|
A:CYS278
|
3.7
|
39.4
|
1.0
|
|
H
|
A:ASN308
|
3.8
|
55.3
|
1.0
|
|
H
|
A:CYS260
|
3.8
|
45.9
|
1.0
|
|
ZN
|
A:ZN503
|
3.8
|
37.6
|
1.0
|
|
HB2
|
A:CYS260
|
3.9
|
55.1
|
1.0
|
|
HB2
|
A:CYS311
|
3.9
|
48.7
|
1.0
|
|
HB2
|
A:CYS307
|
3.9
|
40.0
|
1.0
|
|
N
|
A:CYS260
|
4.0
|
38.3
|
1.0
|
|
CA
|
A:CYS260
|
4.2
|
44.9
|
1.0
|
|
HB3
|
A:CYS278
|
4.2
|
47.3
|
1.0
|
|
H
|
A:CYS278
|
4.3
|
45.9
|
1.0
|
|
SG
|
A:CYS276
|
4.4
|
33.8
|
1.0
|
|
N
|
A:ASN308
|
4.4
|
46.1
|
1.0
|
|
HD22
|
A:ASN319
|
4.5
|
38.8
|
1.0
|
|
N
|
A:CYS307
|
4.5
|
38.8
|
1.0
|
|
HA
|
A:CYS311
|
4.5
|
53.0
|
1.0
|
|
SG
|
A:CYS313
|
4.6
|
41.4
|
1.0
|
|
C
|
A:CYS307
|
4.6
|
43.2
|
1.0
|
|
SG
|
A:CYS268
|
4.6
|
43.9
|
1.0
|
|
CA
|
A:CYS311
|
4.6
|
44.1
|
1.0
|
|
HA2
|
A:GLY259
|
4.7
|
53.3
|
1.0
|
|
C
|
A:GLY259
|
4.8
|
43.7
|
1.0
|
|
H
|
A:CYS307
|
4.9
|
46.6
|
1.0
|
|
N
|
A:CYS278
|
4.9
|
38.3
|
1.0
|
|
CA
|
A:CYS278
|
4.9
|
42.8
|
1.0
|
|
HA
|
A:CYS260
|
4.9
|
53.9
|
1.0
|
|
C
|
A:CYS260
|
5.0
|
53.2
|
1.0
|
|
O
|
A:CYS260
|
5.0
|
47.1
|
1.0
|
|
Zinc binding site 3 out
of 8 in 6box
Go back to
Zinc Binding Sites List in 6box
Zinc binding site 3 out
of 8 in the Structure of the S. Pombe CLR4 Catalytic Domain Bound to Sah
 Mono view
 Stereo pair view
|
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Structure of the S. Pombe CLR4 Catalytic Domain Bound to Sah within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn503
b:37.6
occ:1.00
|
SG
|
A:CYS313
|
2.3
|
41.4
|
1.0
|
|
SG
|
A:CYS307
|
2.3
|
27.3
|
1.0
|
|
SG
|
A:CYS317
|
2.4
|
41.4
|
1.0
|
|
SG
|
A:CYS268
|
2.6
|
43.9
|
1.0
|
|
HB2
|
A:CYS307
|
3.1
|
40.0
|
1.0
|
|
CB
|
A:CYS307
|
3.2
|
33.3
|
1.0
|
|
HB3
|
A:CYS307
|
3.3
|
40.0
|
1.0
|
|
HB3
|
A:CYS313
|
3.4
|
69.1
|
1.0
|
|
CB
|
A:CYS313
|
3.4
|
57.6
|
1.0
|
|
HB2
|
A:CYS317
|
3.4
|
58.8
|
1.0
|
|
CB
|
A:CYS317
|
3.5
|
49.0
|
1.0
|
|
H
|
A:CYS268
|
3.5
|
85.6
|
1.0
|
|
HB2
|
A:CYS313
|
3.6
|
69.1
|
1.0
|
|
HB3
|
A:ASN319
|
3.6
|
41.7
|
1.0
|
|
HB3
|
A:CYS317
|
3.7
|
58.8
|
1.0
|
|
HB2
|
A:CYS268
|
3.7
|
59.4
|
1.0
|
|
ZN
|
A:ZN502
|
3.8
|
31.9
|
1.0
|
|
CB
|
A:CYS268
|
3.8
|
49.5
|
1.0
|
|
ZN
|
A:ZN504
|
3.9
|
44.0
|
1.0
|
|
HE
|
A:ARG320
|
4.1
|
55.1
|
1.0
|
|
HB3
|
A:CYS311
|
4.3
|
48.7
|
1.0
|
|
HB2
|
A:ASN319
|
4.3
|
41.7
|
1.0
|
|
SG
|
A:CYS260
|
4.3
|
44.8
|
1.0
|
|
N
|
A:CYS268
|
4.3
|
71.3
|
1.0
|
|
CB
|
A:ASN319
|
4.4
|
34.7
|
1.0
|
|
HG3
|
A:ARG320
|
4.4
|
50.1
|
1.0
|
|
H
|
A:ASN319
|
4.4
|
47.3
|
1.0
|
|
HD22
|
A:ASN319
|
4.4
|
38.8
|
1.0
|
|
HH21
|
A:ARG320
|
4.5
|
50.3
|
1.0
|
|
HB3
|
A:CYS268
|
4.5
|
59.4
|
1.0
|
|
H
|
A:CYS313
|
4.6
|
70.1
|
1.0
|
|
CA
|
A:CYS307
|
4.6
|
34.2
|
1.0
|
|
NE
|
A:ARG320
|
4.7
|
45.9
|
1.0
|
|
CA
|
A:CYS268
|
4.7
|
66.0
|
1.0
|
|
CA
|
A:CYS313
|
4.8
|
56.9
|
1.0
|
|
H
|
A:CYS307
|
4.8
|
46.6
|
1.0
|
|
HB2
|
A:CYS311
|
4.8
|
48.7
|
1.0
|
|
CA
|
A:CYS317
|
4.9
|
53.1
|
1.0
|
|
CB
|
A:CYS311
|
4.9
|
40.6
|
1.0
|
|
HA
|
A:CYS307
|
4.9
|
41.0
|
1.0
|
|
NH2
|
A:ARG320
|
5.0
|
41.9
|
1.0
|
|
Zinc binding site 4 out
of 8 in 6box
Go back to
Zinc Binding Sites List in 6box
Zinc binding site 4 out
of 8 in the Structure of the S. Pombe CLR4 Catalytic Domain Bound to Sah
 Mono view
 Stereo pair view
|
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of Structure of the S. Pombe CLR4 Catalytic Domain Bound to Sah within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn504
b:44.0
occ:1.00
|
SG
|
A:CYS268
|
2.3
|
43.9
|
1.0
|
|
SG
|
A:CYS276
|
2.3
|
33.8
|
1.0
|
|
SG
|
A:CYS260
|
2.5
|
44.8
|
1.0
|
|
SG
|
A:CYS262
|
2.6
|
50.2
|
1.0
|
|
HB2
|
A:CYS260
|
3.3
|
55.1
|
1.0
|
|
HB2
|
A:CYS262
|
3.4
|
81.8
|
1.0
|
|
HB3
|
A:CYS268
|
3.4
|
59.4
|
1.0
|
|
HB2
|
A:CYS276
|
3.4
|
59.8
|
1.0
|
|
CB
|
A:CYS276
|
3.5
|
49.9
|
1.0
|
|
CB
|
A:CYS260
|
3.5
|
45.9
|
1.0
|
|
CB
|
A:CYS268
|
3.5
|
49.5
|
1.0
|
|
CB
|
A:CYS262
|
3.6
|
68.2
|
1.0
|
|
HA
|
A:CYS276
|
3.6
|
62.7
|
1.0
|
|
ZN
|
A:ZN502
|
3.7
|
31.9
|
1.0
|
|
HB3
|
A:CYS260
|
3.9
|
55.1
|
1.0
|
|
ZN
|
A:ZN503
|
3.9
|
37.6
|
1.0
|
|
SG
|
A:CYS307
|
4.0
|
27.3
|
1.0
|
|
HB3
|
A:CYS262
|
4.0
|
81.8
|
1.0
|
|
CA
|
A:CYS276
|
4.1
|
52.3
|
1.0
|
|
HB2
|
A:CYS268
|
4.1
|
59.4
|
1.0
|
|
HZ
|
A:PHE288
|
4.1
|
47.3
|
1.0
|
|
HB3
|
A:CYS276
|
4.3
|
59.8
|
1.0
|
|
HE1
|
A:PHE288
|
4.4
|
47.4
|
1.0
|
|
HA
|
A:CYS268
|
4.5
|
79.2
|
1.0
|
|
H
|
A:CYS278
|
4.6
|
45.9
|
1.0
|
|
CA
|
A:CYS268
|
4.6
|
66.0
|
1.0
|
|
H
|
A:GLU277
|
4.6
|
53.4
|
1.0
|
|
HB2
|
A:CYS278
|
4.7
|
47.3
|
1.0
|
|
CA
|
A:CYS260
|
4.9
|
44.9
|
1.0
|
|
C
|
A:CYS276
|
4.9
|
50.3
|
1.0
|
|
CZ
|
A:PHE288
|
4.9
|
39.4
|
1.0
|
|
CA
|
A:CYS262
|
4.9
|
70.2
|
1.0
|
|
H
|
A:CYS268
|
4.9
|
85.6
|
1.0
|
|
HB3
|
A:CYS313
|
5.0
|
69.1
|
1.0
|
|
SG
|
A:CYS278
|
5.0
|
22.4
|
1.0
|
|
C
|
A:CYS260
|
5.0
|
53.2
|
1.0
|
|
Zinc binding site 5 out
of 8 in 6box
Go back to
Zinc Binding Sites List in 6box
Zinc binding site 5 out
of 8 in the Structure of the S. Pombe CLR4 Catalytic Domain Bound to Sah
 Mono view
 Stereo pair view
|
|
A full contact list of Zinc with other atoms in the Zn binding
site number 5 of Structure of the S. Pombe CLR4 Catalytic Domain Bound to Sah within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn501
b:41.2
occ:1.00
|
SG
|
B:CYS477
|
2.2
|
39.6
|
1.0
|
|
SG
|
B:CYS479
|
2.3
|
38.9
|
1.0
|
|
SG
|
B:CYS412
|
2.5
|
50.6
|
1.0
|
|
SG
|
B:CYS484
|
2.5
|
46.9
|
1.0
|
|
HB3
|
B:CYS477
|
3.1
|
62.3
|
1.0
|
|
HA
|
B:CYS484
|
3.1
|
55.1
|
1.0
|
|
HB2
|
B:CYS484
|
3.2
|
59.0
|
1.0
|
|
HB2
|
B:CYS412
|
3.2
|
52.9
|
1.0
|
|
H
|
B:CYS412
|
3.2
|
42.7
|
1.0
|
|
CB
|
B:CYS484
|
3.3
|
49.1
|
1.0
|
|
CB
|
B:CYS477
|
3.3
|
51.9
|
1.0
|
|
H
|
B:CYS479
|
3.4
|
51.2
|
1.0
|
|
CB
|
B:CYS412
|
3.5
|
44.1
|
1.0
|
|
HB3
|
B:CYS479
|
3.5
|
50.1
|
1.0
|
|
CB
|
B:CYS479
|
3.6
|
41.8
|
1.0
|
|
H
|
B:GLY486
|
3.6
|
62.1
|
1.0
|
|
HB2
|
B:CYS477
|
3.7
|
62.3
|
1.0
|
|
CA
|
B:CYS484
|
3.7
|
45.9
|
1.0
|
|
HE2
|
B:HIS410
|
3.8
|
51.6
|
1.0
|
|
H
|
B:ARG485
|
3.8
|
58.9
|
1.0
|
|
N
|
B:CYS412
|
3.9
|
35.6
|
1.0
|
|
HD2
|
B:HIS410
|
4.0
|
50.1
|
1.0
|
|
HB2
|
B:SER481
|
4.1
|
57.3
|
1.0
|
|
N
|
B:CYS479
|
4.1
|
42.7
|
1.0
|
|
HB3
|
B:CYS484
|
4.2
|
59.0
|
1.0
|
|
HB3
|
B:CYS412
|
4.2
|
52.9
|
1.0
|
|
H
|
B:SER481
|
4.2
|
52.9
|
1.0
|
|
N
|
B:ARG485
|
4.3
|
49.1
|
1.0
|
|
HB2
|
B:CYS479
|
4.3
|
50.1
|
1.0
|
|
CA
|
B:CYS412
|
4.3
|
37.6
|
1.0
|
|
NE2
|
B:HIS410
|
4.4
|
43.0
|
1.0
|
|
HA
|
B:SER411
|
4.4
|
39.2
|
1.0
|
|
CA
|
B:CYS479
|
4.4
|
43.0
|
1.0
|
|
C
|
B:CYS484
|
4.4
|
47.2
|
1.0
|
|
HG
|
B:SER481
|
4.4
|
62.2
|
1.0
|
|
N
|
B:GLY486
|
4.5
|
51.8
|
1.0
|
|
H
|
B:GLY480
|
4.5
|
55.0
|
1.0
|
|
HN62
|
B:SAH505
|
4.5
|
53.6
|
1.0
|
|
CD2
|
B:HIS410
|
4.5
|
41.8
|
1.0
|
|
CA
|
B:CYS477
|
4.6
|
52.4
|
1.0
|
|
HA2
|
B:GLY486
|
4.6
|
58.8
|
1.0
|
|
C
|
B:CYS477
|
4.7
|
48.0
|
1.0
|
|
HA
|
B:CYS412
|
4.8
|
45.1
|
1.0
|
|
H
|
B:LYS478
|
4.8
|
55.9
|
1.0
|
|
N
|
B:CYS484
|
4.9
|
50.1
|
1.0
|
|
OG
|
B:SER481
|
4.9
|
51.9
|
1.0
|
|
N
|
B:GLY480
|
4.9
|
45.9
|
1.0
|
|
N
|
B:LYS478
|
4.9
|
46.6
|
1.0
|
|
CB
|
B:SER481
|
4.9
|
47.8
|
1.0
|
|
C
|
B:SER411
|
4.9
|
34.4
|
1.0
|
|
HA
|
B:CYS477
|
4.9
|
62.9
|
1.0
|
|
C
|
B:CYS479
|
5.0
|
46.3
|
1.0
|
|
N
|
B:SER481
|
5.0
|
44.1
|
1.0
|
|
Zinc binding site 6 out
of 8 in 6box
Go back to
Zinc Binding Sites List in 6box
Zinc binding site 6 out
of 8 in the Structure of the S. Pombe CLR4 Catalytic Domain Bound to Sah
 Mono view
 Stereo pair view
|
|
A full contact list of Zinc with other atoms in the Zn binding
site number 6 of Structure of the S. Pombe CLR4 Catalytic Domain Bound to Sah within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn502
b:38.8
occ:1.00
|
SG
|
B:CYS313
|
2.3
|
52.1
|
1.0
|
|
SG
|
B:CYS307
|
2.3
|
25.5
|
1.0
|
|
SG
|
B:CYS268
|
2.4
|
48.6
|
1.0
|
|
SG
|
B:CYS317
|
2.5
|
40.6
|
1.0
|
|
HB3
|
B:CYS313
|
3.2
|
67.8
|
1.0
|
|
HB2
|
B:CYS307
|
3.2
|
41.1
|
1.0
|
|
CB
|
B:CYS307
|
3.3
|
34.3
|
1.0
|
|
H
|
B:CYS268
|
3.3
|
80.8
|
1.0
|
|
CB
|
B:CYS313
|
3.3
|
56.5
|
1.0
|
|
HB3
|
B:CYS307
|
3.4
|
41.1
|
1.0
|
|
HB2
|
B:CYS268
|
3.5
|
58.8
|
1.0
|
|
HB2
|
B:CYS317
|
3.5
|
59.4
|
1.0
|
|
HB2
|
B:CYS313
|
3.5
|
67.8
|
1.0
|
|
HB3
|
B:ASN319
|
3.6
|
35.6
|
1.0
|
|
CB
|
B:CYS317
|
3.6
|
49.5
|
1.0
|
|
CB
|
B:CYS268
|
3.6
|
49.0
|
1.0
|
|
HB3
|
B:CYS317
|
3.8
|
59.4
|
1.0
|
|
ZN
|
B:ZN503
|
3.8
|
34.7
|
1.0
|
|
ZN
|
B:ZN504
|
3.9
|
40.4
|
1.0
|
|
N
|
B:CYS268
|
4.1
|
67.3
|
1.0
|
|
SG
|
B:CYS260
|
4.2
|
40.3
|
1.0
|
|
HE
|
B:ARG320
|
4.2
|
68.9
|
1.0
|
|
HB2
|
B:ASN319
|
4.3
|
35.6
|
1.0
|
|
HB3
|
B:CYS311
|
4.3
|
56.7
|
1.0
|
|
HD22
|
B:ASN319
|
4.3
|
27.9
|
1.0
|
|
HB3
|
B:CYS268
|
4.4
|
58.8
|
1.0
|
|
CB
|
B:ASN319
|
4.4
|
29.7
|
1.0
|
|
H
|
B:ASN319
|
4.5
|
40.1
|
1.0
|
|
CA
|
B:CYS268
|
4.5
|
55.4
|
1.0
|
|
H
|
B:CYS313
|
4.5
|
66.4
|
1.0
|
|
HG3
|
B:ARG320
|
4.6
|
48.4
|
1.0
|
|
HH21
|
B:ARG320
|
4.7
|
77.4
|
1.0
|
|
CA
|
B:CYS307
|
4.7
|
35.3
|
1.0
|
|
CA
|
B:CYS313
|
4.7
|
54.3
|
1.0
|
|
HA3
|
B:GLY267
|
4.8
|
96.8
|
1.0
|
|
HB2
|
B:CYS311
|
4.8
|
56.7
|
1.0
|
|
HB2
|
B:CYS262
|
4.9
|
69.6
|
1.0
|
|
H
|
B:CYS307
|
4.9
|
38.3
|
1.0
|
|
HE1
|
B:PHE288
|
4.9
|
44.5
|
1.0
|
|
CB
|
B:CYS311
|
4.9
|
47.2
|
1.0
|
|
HA2
|
B:GLY267
|
4.9
|
96.8
|
1.0
|
|
HA
|
B:CYS307
|
5.0
|
42.3
|
1.0
|
|
HA
|
B:CYS268
|
5.0
|
66.4
|
1.0
|
|
Zinc binding site 7 out
of 8 in 6box
Go back to
Zinc Binding Sites List in 6box
Zinc binding site 7 out
of 8 in the Structure of the S. Pombe CLR4 Catalytic Domain Bound to Sah
 Mono view
 Stereo pair view
|
|
A full contact list of Zinc with other atoms in the Zn binding
site number 7 of Structure of the S. Pombe CLR4 Catalytic Domain Bound to Sah within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn503
b:34.7
occ:1.00
|
SG
|
B:CYS307
|
2.3
|
25.5
|
1.0
|
|
SG
|
B:CYS311
|
2.4
|
41.2
|
1.0
|
|
SG
|
B:CYS260
|
2.4
|
40.3
|
1.0
|
|
SG
|
B:CYS278
|
2.4
|
30.5
|
1.0
|
|
HB3
|
B:CYS260
|
2.7
|
52.4
|
1.0
|
|
HB3
|
B:CYS307
|
3.0
|
41.1
|
1.0
|
|
HA
|
B:CYS307
|
3.0
|
42.3
|
1.0
|
|
CB
|
B:CYS307
|
3.1
|
34.3
|
1.0
|
|
CB
|
B:CYS260
|
3.1
|
43.7
|
1.0
|
|
HB3
|
B:CYS311
|
3.1
|
56.7
|
1.0
|
|
CB
|
B:CYS311
|
3.4
|
47.2
|
1.0
|
|
CA
|
B:CYS307
|
3.6
|
35.3
|
1.0
|
|
ZN
|
B:ZN504
|
3.7
|
40.4
|
1.0
|
|
HB2
|
B:CYS278
|
3.7
|
54.9
|
1.0
|
|
HB2
|
B:CYS260
|
3.8
|
52.4
|
1.0
|
|
ZN
|
B:ZN502
|
3.8
|
38.8
|
1.0
|
|
CB
|
B:CYS278
|
3.8
|
45.7
|
1.0
|
|
H
|
B:ASN308
|
3.8
|
63.6
|
1.0
|
|
HB2
|
B:CYS311
|
3.9
|
56.7
|
1.0
|
|
H
|
B:CYS260
|
3.9
|
52.6
|
1.0
|
|
SG
|
B:CYS276
|
3.9
|
27.4
|
1.0
|
|
HB2
|
B:CYS307
|
4.0
|
41.1
|
1.0
|
|
N
|
B:CYS260
|
4.1
|
43.9
|
1.0
|
|
CA
|
B:CYS260
|
4.2
|
46.7
|
1.0
|
|
H
|
B:CYS278
|
4.3
|
50.7
|
1.0
|
|
HB3
|
B:CYS278
|
4.3
|
54.9
|
1.0
|
|
N
|
B:ASN308
|
4.5
|
53.0
|
1.0
|
|
HD22
|
B:ASN319
|
4.5
|
27.9
|
1.0
|
|
SG
|
B:CYS268
|
4.5
|
48.6
|
1.0
|
|
N
|
B:CYS307
|
4.5
|
31.9
|
1.0
|
|
HA
|
B:CYS311
|
4.5
|
58.7
|
1.0
|
|
SG
|
B:CYS313
|
4.6
|
52.1
|
1.0
|
|
C
|
B:CYS307
|
4.6
|
44.0
|
1.0
|
|
CA
|
B:CYS311
|
4.6
|
48.9
|
1.0
|
|
HA2
|
B:GLY259
|
4.7
|
57.6
|
1.0
|
|
C
|
B:GLY259
|
4.8
|
49.8
|
1.0
|
|
H
|
B:CYS307
|
4.9
|
38.3
|
1.0
|
|
HA
|
B:CYS260
|
4.9
|
56.1
|
1.0
|
|
N
|
B:CYS278
|
4.9
|
42.2
|
1.0
|
|
CA
|
B:CYS278
|
5.0
|
43.3
|
1.0
|
|
Zinc binding site 8 out
of 8 in 6box
Go back to
Zinc Binding Sites List in 6box
Zinc binding site 8 out
of 8 in the Structure of the S. Pombe CLR4 Catalytic Domain Bound to Sah
 Mono view
 Stereo pair view
|
|
A full contact list of Zinc with other atoms in the Zn binding
site number 8 of Structure of the S. Pombe CLR4 Catalytic Domain Bound to Sah within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn504
b:40.4
occ:1.00
|
SG
|
B:CYS268
|
2.2
|
48.6
|
1.0
|
|
SG
|
B:CYS276
|
2.3
|
27.4
|
1.0
|
|
SG
|
B:CYS260
|
2.6
|
40.3
|
1.0
|
|
SG
|
B:CYS262
|
2.7
|
47.1
|
1.0
|
|
HB2
|
B:CYS276
|
2.9
|
61.2
|
1.0
|
|
CB
|
B:CYS276
|
3.1
|
51.0
|
1.0
|
|
HB3
|
B:CYS268
|
3.2
|
58.8
|
1.0
|
|
HB2
|
B:CYS260
|
3.3
|
52.4
|
1.0
|
|
HA
|
B:CYS276
|
3.3
|
59.7
|
1.0
|
|
CB
|
B:CYS268
|
3.4
|
49.0
|
1.0
|
|
HB2
|
B:CYS262
|
3.4
|
69.6
|
1.0
|
|
CB
|
B:CYS260
|
3.5
|
43.7
|
1.0
|
|
CB
|
B:CYS262
|
3.7
|
58.0
|
1.0
|
|
ZN
|
B:ZN503
|
3.7
|
34.7
|
1.0
|
|
CA
|
B:CYS276
|
3.8
|
49.7
|
1.0
|
|
HB3
|
B:CYS260
|
3.9
|
52.4
|
1.0
|
|
ZN
|
B:ZN502
|
3.9
|
38.8
|
1.0
|
|
HB2
|
B:CYS268
|
3.9
|
58.8
|
1.0
|
|
HZ
|
B:PHE288
|
3.9
|
47.3
|
1.0
|
|
HB3
|
B:CYS276
|
4.0
|
61.2
|
1.0
|
|
SG
|
B:CYS307
|
4.0
|
25.5
|
1.0
|
|
HB3
|
B:CYS262
|
4.1
|
69.6
|
1.0
|
|
HE1
|
B:PHE288
|
4.2
|
44.5
|
1.0
|
|
HA
|
B:CYS268
|
4.4
|
66.4
|
1.0
|
|
H
|
B:GLU277
|
4.5
|
55.4
|
1.0
|
|
CA
|
B:CYS268
|
4.5
|
55.4
|
1.0
|
|
H
|
B:CYS278
|
4.6
|
50.7
|
1.0
|
|
CZ
|
B:PHE288
|
4.7
|
39.5
|
1.0
|
|
C
|
B:CYS276
|
4.7
|
49.1
|
1.0
|
|
HB2
|
B:CYS278
|
4.8
|
54.9
|
1.0
|
|
CE1
|
B:PHE288
|
4.8
|
37.0
|
1.0
|
|
N
|
B:GLU277
|
4.8
|
46.1
|
1.0
|
|
N
|
B:CYS276
|
4.9
|
52.7
|
1.0
|
|
H
|
B:CYS268
|
4.9
|
80.8
|
1.0
|
|
CA
|
B:CYS260
|
4.9
|
46.7
|
1.0
|
|
CA
|
B:CYS262
|
5.0
|
61.7
|
1.0
|
|
Reference:
N.Iglesias,
M.A.Currie,
G.Jih,
J.A.Paulo,
N.Siuti,
M.Kalocsay,
S.P.Gygi,
D.Moazed.
Automethylation-Induced Conformational Switch in CLR4 (SUV39H) Maintains Epigenetic Stability. Nature V. 560 504 2018.
ISSN: ESSN 1476-4687
PubMed: 30051891
DOI: 10.1038/S41586-018-0398-2
Page generated: Wed Dec 16 11:32:51 2020
|
