Zinc in PDB 2o8j: Human Euchromatic Histone Methyltransferase 2
Enzymatic activity of Human Euchromatic Histone Methyltransferase 2
All present enzymatic activity of Human Euchromatic Histone Methyltransferase 2:
2.1.1.43;
Protein crystallography data
The structure of Human Euchromatic Histone Methyltransferase 2, PDB code: 2o8j
was solved by
J.Min,
H.Wu,
T.Antoshenko,
P.Loppnau,
J.Weigelt,
M.Sundstrom,
C.H.Arrowsmith,
A.M.Edwards,
A.Bochkarev,
A.N.Plotnikov,
Structural Genomics Consortium (Sgc),
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
79.31 /
1.80
|
Space group
|
P 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
56.586,
70.965,
83.046,
81.11,
75.13,
88.39
|
R / Rfree (%)
|
18.2 /
22.1
|
Zinc Binding Sites:
Pages:
>>> Page 1 <<<
Page 2, Binding sites: 11 -
16;
Binding sites:
The binding sites of Zinc atom in the Human Euchromatic Histone Methyltransferase 2
(pdb code 2o8j). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 16 binding sites of Zinc where determined in the
Human Euchromatic Histone Methyltransferase 2, PDB code: 2o8j:
Jump to Zinc binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Zinc binding site 1 out
of 16 in 2o8j
Go back to
Zinc Binding Sites List in 2o8j
Zinc binding site 1 out
of 16 in the Human Euchromatic Histone Methyltransferase 2
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Human Euchromatic Histone Methyltransferase 2 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn1501
b:18.4
occ:1.00
|
SG
|
A:CYS987
|
2.3
|
16.9
|
1.0
|
SG
|
A:CYS1021
|
2.3
|
14.4
|
1.0
|
SG
|
A:CYS1017
|
2.4
|
14.9
|
1.0
|
SG
|
A:CYS974
|
2.5
|
14.9
|
1.0
|
CB
|
A:CYS1017
|
3.2
|
15.6
|
1.0
|
CB
|
A:CYS974
|
3.3
|
15.6
|
1.0
|
CB
|
A:CYS1021
|
3.3
|
15.0
|
1.0
|
CB
|
A:CYS987
|
3.4
|
18.1
|
1.0
|
N
|
A:CYS974
|
3.6
|
15.7
|
1.0
|
CA
|
A:CYS1017
|
3.6
|
14.9
|
1.0
|
ZN
|
A:ZN1503
|
3.8
|
18.0
|
1.0
|
ZN
|
A:ZN1502
|
3.8
|
17.6
|
1.0
|
CA
|
A:CYS974
|
4.0
|
15.5
|
1.0
|
SG
|
A:CYS1023
|
4.2
|
15.6
|
1.0
|
SG
|
A:CYS985
|
4.3
|
17.9
|
1.0
|
N
|
A:CYS1017
|
4.5
|
13.2
|
1.0
|
N
|
A:ASN1018
|
4.6
|
14.9
|
1.0
|
C
|
A:HIS973
|
4.6
|
15.9
|
1.0
|
CA
|
A:CYS1021
|
4.6
|
13.6
|
1.0
|
CA
|
A:CYS987
|
4.7
|
19.5
|
1.0
|
C
|
A:CYS1017
|
4.7
|
16.0
|
1.0
|
N
|
A:CYS987
|
4.7
|
19.1
|
1.0
|
SG
|
A:CYS980
|
4.7
|
16.1
|
1.0
|
CA
|
A:HIS973
|
4.8
|
15.6
|
1.0
|
C
|
A:CYS974
|
4.8
|
15.7
|
1.0
|
O
|
A:HOH1520
|
4.9
|
17.1
|
1.0
|
O
|
A:CYS974
|
4.9
|
15.1
|
1.0
|
ND2
|
A:ASN1029
|
5.0
|
16.3
|
1.0
|
|
Zinc binding site 2 out
of 16 in 2o8j
Go back to
Zinc Binding Sites List in 2o8j
Zinc binding site 2 out
of 16 in the Human Euchromatic Histone Methyltransferase 2
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Human Euchromatic Histone Methyltransferase 2 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn1502
b:17.6
occ:1.00
|
SG
|
A:CYS1027
|
2.3
|
16.9
|
1.0
|
SG
|
A:CYS980
|
2.3
|
16.1
|
1.0
|
SG
|
A:CYS1023
|
2.3
|
15.6
|
1.0
|
SG
|
A:CYS1017
|
2.4
|
14.9
|
1.0
|
CB
|
A:CYS1017
|
3.1
|
15.6
|
1.0
|
CB
|
A:CYS1027
|
3.2
|
17.1
|
1.0
|
CB
|
A:CYS1023
|
3.2
|
16.2
|
1.0
|
CB
|
A:CYS980
|
3.3
|
17.2
|
1.0
|
ZN
|
A:ZN1503
|
3.8
|
18.0
|
1.0
|
ZN
|
A:ZN1501
|
3.8
|
18.4
|
1.0
|
SG
|
A:CYS974
|
4.1
|
14.9
|
1.0
|
NE
|
A:ARG1030
|
4.3
|
18.3
|
1.0
|
NH2
|
A:ARG1030
|
4.5
|
19.2
|
1.0
|
CB
|
A:ASN1029
|
4.5
|
16.6
|
1.0
|
CA
|
A:CYS1017
|
4.6
|
14.9
|
1.0
|
CA
|
A:CYS1023
|
4.6
|
14.9
|
1.0
|
CA
|
A:CYS1027
|
4.7
|
17.4
|
1.0
|
CA
|
A:CYS980
|
4.7
|
17.4
|
1.0
|
O
|
A:TRP1024
|
4.7
|
18.1
|
1.0
|
CZ
|
A:ARG1030
|
4.8
|
20.9
|
1.0
|
N
|
A:ASN1029
|
5.0
|
15.9
|
1.0
|
CB
|
A:CYS1021
|
5.0
|
15.0
|
1.0
|
N
|
A:CYS980
|
5.0
|
16.8
|
1.0
|
|
Zinc binding site 3 out
of 16 in 2o8j
Go back to
Zinc Binding Sites List in 2o8j
Zinc binding site 3 out
of 16 in the Human Euchromatic Histone Methyltransferase 2
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Human Euchromatic Histone Methyltransferase 2 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn1503
b:18.0
occ:1.00
|
SG
|
A:CYS985
|
2.3
|
17.9
|
1.0
|
SG
|
A:CYS974
|
2.3
|
14.9
|
1.0
|
SG
|
A:CYS980
|
2.4
|
16.1
|
1.0
|
SG
|
A:CYS976
|
2.4
|
16.2
|
1.0
|
CB
|
A:CYS974
|
3.1
|
15.6
|
1.0
|
CB
|
A:CYS976
|
3.2
|
16.2
|
1.0
|
CB
|
A:CYS985
|
3.3
|
18.6
|
1.0
|
CB
|
A:CYS980
|
3.4
|
17.2
|
1.0
|
ZN
|
A:ZN1501
|
3.8
|
18.4
|
1.0
|
ZN
|
A:ZN1502
|
3.8
|
17.6
|
1.0
|
CA
|
A:CYS985
|
3.9
|
19.3
|
1.0
|
CA
|
A:CYS980
|
4.0
|
17.4
|
1.0
|
SG
|
A:CYS1017
|
4.1
|
14.9
|
1.0
|
N
|
A:CYS976
|
4.4
|
16.0
|
1.0
|
CA
|
A:CYS976
|
4.4
|
15.8
|
1.0
|
CA
|
A:CYS974
|
4.6
|
15.5
|
1.0
|
C
|
A:CYS985
|
4.7
|
19.2
|
1.0
|
O
|
A:HOH1548
|
4.7
|
20.7
|
1.0
|
O
|
A:HOH1544
|
4.7
|
18.4
|
1.0
|
N
|
A:LEU986
|
4.7
|
19.3
|
1.0
|
SG
|
A:CYS1023
|
4.8
|
15.6
|
1.0
|
N
|
A:CYS980
|
4.8
|
16.8
|
1.0
|
CB
|
A:CYS1023
|
4.9
|
16.2
|
1.0
|
O
|
A:HOH1545
|
4.9
|
21.2
|
1.0
|
|
Zinc binding site 4 out
of 16 in 2o8j
Go back to
Zinc Binding Sites List in 2o8j
Zinc binding site 4 out
of 16 in the Human Euchromatic Histone Methyltransferase 2
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of Human Euchromatic Histone Methyltransferase 2 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn1504
b:27.3
occ:1.00
|
SG
|
A:CYS1168
|
2.2
|
25.4
|
1.0
|
SG
|
A:CYS1170
|
2.3
|
27.9
|
1.0
|
SG
|
A:CYS1175
|
2.4
|
28.6
|
1.0
|
SG
|
A:CYS1115
|
2.5
|
26.5
|
1.0
|
CB
|
A:CYS1175
|
3.1
|
30.9
|
1.0
|
CB
|
A:CYS1170
|
3.2
|
28.7
|
1.0
|
CB
|
A:CYS1168
|
3.3
|
28.1
|
1.0
|
CB
|
A:CYS1115
|
3.4
|
23.6
|
1.0
|
CA
|
A:CYS1175
|
3.7
|
31.7
|
1.0
|
N
|
A:CYS1170
|
4.0
|
28.2
|
1.0
|
N
|
A:CYS1115
|
4.1
|
22.9
|
1.0
|
O
|
A:HOH1558
|
4.1
|
24.1
|
1.0
|
CA
|
A:CYS1170
|
4.2
|
29.2
|
1.0
|
N
|
A:LYS1176
|
4.3
|
31.3
|
1.0
|
CA
|
A:CYS1115
|
4.4
|
23.7
|
1.0
|
C
|
A:CYS1175
|
4.4
|
31.9
|
1.0
|
N
|
A:HIS1177
|
4.5
|
29.2
|
1.0
|
CA
|
A:CYS1168
|
4.6
|
28.3
|
1.0
|
CE1
|
A:HIS1113
|
4.6
|
22.1
|
1.0
|
ND1
|
A:HIS1113
|
4.6
|
22.0
|
1.0
|
C
|
A:CYS1168
|
4.7
|
28.7
|
1.0
|
N
|
A:GLY1171
|
4.7
|
31.8
|
1.0
|
C
|
A:CYS1170
|
4.8
|
30.1
|
1.0
|
CB
|
A:HIS1177
|
4.8
|
29.0
|
1.0
|
N
|
A:CYS1175
|
4.8
|
32.5
|
1.0
|
N
|
A:SER1178
|
4.9
|
29.4
|
1.0
|
N
|
A:GLN1169
|
5.0
|
28.5
|
1.0
|
|
Zinc binding site 5 out
of 16 in 2o8j
Go back to
Zinc Binding Sites List in 2o8j
Zinc binding site 5 out
of 16 in the Human Euchromatic Histone Methyltransferase 2
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 5 of Human Euchromatic Histone Methyltransferase 2 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn1505
b:26.3
occ:1.00
|
SG
|
B:CYS1017
|
2.3
|
23.1
|
1.0
|
SG
|
B:CYS1021
|
2.4
|
20.0
|
1.0
|
SG
|
B:CYS974
|
2.4
|
24.5
|
1.0
|
SG
|
B:CYS987
|
2.4
|
27.0
|
1.0
|
CB
|
B:CYS1017
|
3.2
|
20.2
|
1.0
|
CB
|
B:CYS974
|
3.3
|
26.5
|
1.0
|
CB
|
B:CYS1021
|
3.3
|
21.1
|
1.0
|
CB
|
B:CYS987
|
3.5
|
28.1
|
1.0
|
CA
|
B:CYS1017
|
3.6
|
19.7
|
1.0
|
N
|
B:CYS974
|
3.6
|
27.2
|
1.0
|
ZN
|
B:ZN1507
|
3.7
|
27.9
|
1.0
|
ZN
|
B:ZN1506
|
3.8
|
25.0
|
1.0
|
CA
|
B:CYS974
|
4.1
|
27.1
|
1.0
|
SG
|
B:CYS1023
|
4.1
|
21.2
|
1.0
|
SG
|
B:CYS985
|
4.3
|
26.3
|
1.0
|
SG
|
B:CYS980
|
4.5
|
24.5
|
1.0
|
N
|
B:CYS1017
|
4.5
|
19.8
|
1.0
|
N
|
B:ASN1018
|
4.6
|
17.9
|
1.0
|
CA
|
B:CYS1021
|
4.6
|
20.9
|
1.0
|
C
|
B:HIS973
|
4.6
|
28.2
|
1.0
|
C
|
B:CYS1017
|
4.7
|
19.1
|
1.0
|
CA
|
B:CYS987
|
4.7
|
28.2
|
1.0
|
N
|
B:CYS987
|
4.7
|
28.9
|
1.0
|
CA
|
B:HIS973
|
4.8
|
28.3
|
1.0
|
ND2
|
B:ASN1029
|
4.9
|
20.6
|
1.0
|
C
|
B:CYS974
|
4.9
|
28.0
|
1.0
|
O
|
B:HOH1535
|
4.9
|
22.9
|
1.0
|
|
Zinc binding site 6 out
of 16 in 2o8j
Go back to
Zinc Binding Sites List in 2o8j
Zinc binding site 6 out
of 16 in the Human Euchromatic Histone Methyltransferase 2
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 6 of Human Euchromatic Histone Methyltransferase 2 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn1506
b:25.0
occ:1.00
|
SG
|
B:CYS1027
|
2.2
|
23.6
|
1.0
|
SG
|
B:CYS1017
|
2.4
|
23.1
|
1.0
|
SG
|
B:CYS1023
|
2.4
|
21.2
|
1.0
|
SG
|
B:CYS980
|
2.6
|
24.5
|
1.0
|
CB
|
B:CYS1017
|
3.1
|
20.2
|
1.0
|
CB
|
B:CYS1027
|
3.2
|
24.7
|
1.0
|
CB
|
B:CYS980
|
3.2
|
29.3
|
1.0
|
CB
|
B:CYS1023
|
3.2
|
23.2
|
1.0
|
ZN
|
B:ZN1507
|
3.8
|
27.9
|
1.0
|
ZN
|
B:ZN1505
|
3.8
|
26.3
|
1.0
|
SG
|
B:CYS974
|
4.2
|
24.5
|
1.0
|
NE
|
B:ARG1030
|
4.3
|
24.9
|
1.0
|
NH2
|
B:ARG1030
|
4.4
|
22.4
|
1.0
|
CB
|
B:ASN1029
|
4.5
|
21.9
|
1.0
|
CA
|
B:CYS1017
|
4.6
|
19.7
|
1.0
|
CA
|
B:CYS980
|
4.7
|
30.1
|
1.0
|
CA
|
B:CYS1027
|
4.7
|
24.4
|
1.0
|
CA
|
B:CYS1023
|
4.7
|
22.4
|
1.0
|
CZ
|
B:ARG1030
|
4.8
|
23.8
|
1.0
|
O
|
B:TRP1024
|
4.8
|
23.9
|
1.0
|
N
|
B:ASN1029
|
4.9
|
23.3
|
1.0
|
|
Zinc binding site 7 out
of 16 in 2o8j
Go back to
Zinc Binding Sites List in 2o8j
Zinc binding site 7 out
of 16 in the Human Euchromatic Histone Methyltransferase 2
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 7 of Human Euchromatic Histone Methyltransferase 2 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn1507
b:27.9
occ:1.00
|
SG
|
B:CYS980
|
2.0
|
24.5
|
1.0
|
SG
|
B:CYS974
|
2.4
|
24.5
|
1.0
|
SG
|
B:CYS985
|
2.4
|
26.3
|
1.0
|
SG
|
B:CYS976
|
2.5
|
27.6
|
1.0
|
CB
|
B:CYS976
|
3.1
|
31.9
|
1.0
|
CB
|
B:CYS974
|
3.2
|
26.5
|
1.0
|
CB
|
B:CYS980
|
3.3
|
29.3
|
1.0
|
CB
|
B:CYS985
|
3.3
|
30.8
|
1.0
|
ZN
|
B:ZN1505
|
3.7
|
26.3
|
1.0
|
ZN
|
B:ZN1506
|
3.8
|
25.0
|
1.0
|
CA
|
B:CYS980
|
3.9
|
30.1
|
1.0
|
CA
|
B:CYS985
|
4.0
|
30.9
|
1.0
|
SG
|
B:CYS1017
|
4.0
|
23.1
|
1.0
|
CA
|
B:CYS976
|
4.4
|
31.7
|
1.0
|
N
|
B:CYS976
|
4.5
|
30.7
|
1.0
|
O
|
B:HOH1530
|
4.6
|
29.5
|
1.0
|
CA
|
B:CYS974
|
4.7
|
27.1
|
1.0
|
C
|
B:CYS985
|
4.7
|
30.7
|
1.0
|
SG
|
B:CYS1023
|
4.8
|
21.2
|
1.0
|
N
|
B:CYS980
|
4.8
|
30.5
|
1.0
|
CB
|
B:CYS1023
|
4.8
|
23.2
|
1.0
|
N
|
B:LEU986
|
4.9
|
30.1
|
1.0
|
C
|
B:CYS980
|
5.0
|
31.9
|
1.0
|
|
Zinc binding site 8 out
of 16 in 2o8j
Go back to
Zinc Binding Sites List in 2o8j
Zinc binding site 8 out
of 16 in the Human Euchromatic Histone Methyltransferase 2
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 8 of Human Euchromatic Histone Methyltransferase 2 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn1508
b:29.2
occ:1.00
|
SG
|
B:CYS1170
|
2.3
|
30.9
|
1.0
|
SG
|
B:CYS1115
|
2.3
|
29.8
|
1.0
|
SG
|
B:CYS1168
|
2.4
|
28.6
|
1.0
|
SG
|
B:CYS1175
|
2.4
|
32.9
|
1.0
|
CB
|
B:CYS1115
|
3.2
|
29.3
|
1.0
|
CB
|
B:CYS1175
|
3.2
|
35.5
|
1.0
|
CB
|
B:CYS1170
|
3.3
|
33.3
|
1.0
|
CB
|
B:CYS1168
|
3.4
|
29.5
|
1.0
|
CA
|
B:CYS1175
|
3.7
|
35.2
|
1.0
|
N
|
B:CYS1115
|
4.0
|
27.9
|
1.0
|
N
|
B:CYS1170
|
4.0
|
32.1
|
1.0
|
CA
|
B:CYS1170
|
4.2
|
33.6
|
1.0
|
O
|
B:HOH1582
|
4.2
|
33.6
|
1.0
|
CA
|
B:CYS1115
|
4.2
|
29.2
|
1.0
|
N
|
B:LYS1176
|
4.2
|
34.2
|
1.0
|
C
|
B:CYS1175
|
4.4
|
34.7
|
1.0
|
CE1
|
B:HIS1113
|
4.4
|
21.8
|
1.0
|
N
|
B:HIS1177
|
4.5
|
32.0
|
1.0
|
ND1
|
B:HIS1113
|
4.6
|
24.5
|
1.0
|
CA
|
B:CYS1168
|
4.6
|
29.7
|
1.0
|
C
|
B:CYS1168
|
4.7
|
30.4
|
1.0
|
N
|
B:GLY1171
|
4.8
|
35.9
|
1.0
|
C
|
B:CYS1170
|
4.9
|
34.5
|
1.0
|
N
|
B:CYS1175
|
4.9
|
35.9
|
1.0
|
O
|
B:CYS1168
|
4.9
|
30.4
|
1.0
|
CB
|
B:HIS1177
|
5.0
|
31.6
|
1.0
|
|
Zinc binding site 9 out
of 16 in 2o8j
Go back to
Zinc Binding Sites List in 2o8j
Zinc binding site 9 out
of 16 in the Human Euchromatic Histone Methyltransferase 2
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 9 of Human Euchromatic Histone Methyltransferase 2 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn1509
b:17.4
occ:1.00
|
SG
|
C:CYS987
|
2.3
|
15.4
|
1.0
|
SG
|
C:CYS1021
|
2.3
|
13.9
|
1.0
|
SG
|
C:CYS1017
|
2.4
|
12.8
|
1.0
|
SG
|
C:CYS974
|
2.4
|
13.4
|
1.0
|
CB
|
C:CYS1017
|
3.2
|
13.7
|
1.0
|
CB
|
C:CYS974
|
3.3
|
13.7
|
1.0
|
CB
|
C:CYS1021
|
3.3
|
13.1
|
1.0
|
CB
|
C:CYS987
|
3.4
|
16.0
|
1.0
|
N
|
C:CYS974
|
3.5
|
14.8
|
1.0
|
CA
|
C:CYS1017
|
3.6
|
13.1
|
1.0
|
ZN
|
C:ZN1511
|
3.8
|
16.9
|
1.0
|
ZN
|
C:ZN1510
|
3.8
|
16.0
|
1.0
|
CA
|
C:CYS974
|
4.0
|
14.7
|
1.0
|
SG
|
C:CYS1023
|
4.2
|
13.6
|
1.0
|
SG
|
C:CYS985
|
4.3
|
16.5
|
1.0
|
N
|
C:CYS1017
|
4.5
|
11.8
|
1.0
|
N
|
C:ASN1018
|
4.5
|
14.1
|
1.0
|
C
|
C:HIS973
|
4.6
|
16.3
|
1.0
|
CA
|
C:CYS987
|
4.6
|
17.4
|
1.0
|
C
|
C:CYS1017
|
4.6
|
13.2
|
1.0
|
CA
|
C:CYS1021
|
4.6
|
14.1
|
1.0
|
N
|
C:CYS987
|
4.7
|
16.1
|
1.0
|
SG
|
C:CYS980
|
4.7
|
14.8
|
1.0
|
CA
|
C:HIS973
|
4.8
|
16.1
|
1.0
|
C
|
C:CYS974
|
4.9
|
14.2
|
1.0
|
O
|
C:HOH1548
|
4.9
|
14.3
|
1.0
|
O
|
C:CYS974
|
5.0
|
13.0
|
1.0
|
|
Zinc binding site 10 out
of 16 in 2o8j
Go back to
Zinc Binding Sites List in 2o8j
Zinc binding site 10 out
of 16 in the Human Euchromatic Histone Methyltransferase 2
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 10 of Human Euchromatic Histone Methyltransferase 2 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn1510
b:16.0
occ:1.00
|
SG
|
C:CYS1023
|
2.3
|
13.6
|
1.0
|
SG
|
C:CYS1027
|
2.3
|
14.8
|
1.0
|
SG
|
C:CYS980
|
2.4
|
14.8
|
1.0
|
SG
|
C:CYS1017
|
2.4
|
12.8
|
1.0
|
CB
|
C:CYS1017
|
3.1
|
13.7
|
1.0
|
CB
|
C:CYS1023
|
3.2
|
14.9
|
1.0
|
CB
|
C:CYS1027
|
3.2
|
15.9
|
1.0
|
CB
|
C:CYS980
|
3.3
|
13.7
|
1.0
|
ZN
|
C:ZN1511
|
3.8
|
16.9
|
1.0
|
ZN
|
C:ZN1509
|
3.8
|
17.4
|
1.0
|
SG
|
C:CYS974
|
4.1
|
13.4
|
1.0
|
NE
|
C:ARG1030
|
4.3
|
18.4
|
1.0
|
NH2
|
C:ARG1030
|
4.4
|
18.6
|
1.0
|
CB
|
C:ASN1029
|
4.6
|
13.3
|
1.0
|
CA
|
C:CYS1017
|
4.6
|
13.1
|
1.0
|
CA
|
C:CYS1023
|
4.6
|
13.7
|
1.0
|
CA
|
C:CYS1027
|
4.7
|
16.0
|
1.0
|
CA
|
C:CYS980
|
4.7
|
15.3
|
1.0
|
CZ
|
C:ARG1030
|
4.8
|
19.4
|
1.0
|
O
|
C:TRP1024
|
4.8
|
17.4
|
1.0
|
N
|
C:ASN1029
|
5.0
|
13.2
|
1.0
|
CB
|
C:CYS1021
|
5.0
|
13.1
|
1.0
|
N
|
C:CYS980
|
5.0
|
14.3
|
1.0
|
|
Reference:
H.Wu,
J.Min,
V.V.Lunin,
T.Antoshenko,
L.Dombrovski,
H.Zeng,
A.Allali-Hassani,
V.Campagna-Slater,
M.Vedadi,
C.H.Arrowsmith,
A.N.Plotnikov,
M.Schapira.
Structural Biology of Human H3K9 Methyltransferases Plos One V. 5 E8570 2010.
ISSN: ESSN 1932-6203
PubMed: 20084102
DOI: 10.1371/JOURNAL.PONE.0008570
Page generated: Thu Oct 17 02:31:35 2024
|