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DNA (cytosine-5)-methyltransferase 3-like

Intramolecular
Cysteine 108 and cysteine 113
Cysteine 73 and cysteine 76
Cysteine 113 and cysteine 142
Cysteine 99 and cysteine 118
Cysteine 56 and cysteine 76
Cysteine 118 and cysteine 121
Cysteine 56 and cysteine 73
Cysteine 53 and cysteine 73
Cysteine 53 and cysteine 56
Cysteine 108 and cysteine 145
More...
Cysteine 53 and cysteine 76
Cysteine 55 and cysteine 76
Cysteine 142 and cysteine 145
Cysteine 113 and cysteine 145
Cysteine 96 and cysteine 121
Cysteine 96 and cysteine 118
Cysteine 96 and cysteine 99
Cysteine 55 and cysteine 56
Cysteine 76 and cysteine 99
Cysteine 99 and cysteine 100
Cysteine 53 and cysteine 121
Cysteine 55 and cysteine 100
Cysteine 96 and cysteine 100
Cysteine 100 and cysteine 118
Cysteine 108 and cysteine 142
Cysteine 55 and cysteine 73
Cysteine 76 and cysteine 100
Cysteine 55 and cysteine 118
Cysteine 113 and cysteine 116
Cysteine 99 and cysteine 121
Cysteine 53 and cysteine 55
Cysteine 53 and cysteine 99
Cysteine 96 and cysteine 116
Cysteine 55 and cysteine 99
Cysteine 116 and cysteine 142
Cysteine 108 and cysteine 116
Cysteine 116 and cysteine 118
Cysteine 100 and cysteine 121
Cysteine 56 and cysteine 99
Cysteine 53 and cysteine 100
A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3-like between cysteines 108 and 113.

Details

Redox score ?
91
PDB code
2pv0
Structure name
dna methyltransferase 3 like protein (dnmt3l)
Structure deposition date
2007-05-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
1
% buried
55
Peptide accession
Q9UJW3
Residue number A
108
Residue number B
113
Peptide name
DNA (cytosine-5)-methyltransferase 3-like

Ligandability

Cysteine 108 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 113 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3-like between cysteines 73 and 76.

Details

Redox score ?
87
PDB code
2pvc
Structure name
dnmt3l recognizes unmethylated histone h3 lysine 4
Structure deposition date
2007-05-09
Thiol separation (Å)
3
Half-sphere exposure sum ?
56
Minimum pKa ?
5
% buried
26
Peptide accession
Q9UJW3
Residue number A
73
Residue number B
76
Peptide name
DNA (cytosine-5)-methyltransferase 3-like

Ligandability

Cysteine 73 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 76 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3-like between cysteines 113 and 142.

Details

Redox score ?
81
PDB code
2pvc
Structure name
dnmt3l recognizes unmethylated histone h3 lysine 4
Structure deposition date
2007-05-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
71
Minimum pKa ?
5
% buried
95
Peptide accession
Q9UJW3
Residue number A
113
Residue number B
142
Peptide name
DNA (cytosine-5)-methyltransferase 3-like

Ligandability

Cysteine 113 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 142 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3-like between cysteines 99 and 118.

Details

Redox score ?
80
PDB code
2pvc
Structure name
dnmt3l recognizes unmethylated histone h3 lysine 4
Structure deposition date
2007-05-09
Thiol separation (Å)
3
Half-sphere exposure sum ?
87
Minimum pKa ?
5
% buried
90
Peptide accession
Q9UJW3
Residue number A
99
Residue number B
118
Peptide name
DNA (cytosine-5)-methyltransferase 3-like

Ligandability

Cysteine 99 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 118 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3-like between cysteines 56 and 76.

Details

Redox score ?
75
PDB code
2pvc
Structure name
dnmt3l recognizes unmethylated histone h3 lysine 4
Structure deposition date
2007-05-09
Thiol separation (Å)
3
Half-sphere exposure sum ?
63
Minimum pKa ?
10
% buried
36
Peptide accession
Q9UJW3
Residue number A
56
Residue number B
76
Peptide name
DNA (cytosine-5)-methyltransferase 3-like

Ligandability

Cysteine 56 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 76 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3-like between cysteines 118 and 121.

Details

Redox score ?
74
PDB code
2pv0
Structure name
dna methyltransferase 3 like protein (dnmt3l)
Structure deposition date
2007-05-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
82
Minimum pKa ?
5
% buried
87
Peptide accession
Q9UJW3
Residue number A
118
Residue number B
121
Peptide name
DNA (cytosine-5)-methyltransferase 3-like

Ligandability

Cysteine 118 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 121 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3-like between cysteines 56 and 73.

Details

Redox score ?
74
PDB code
2pv0
Structure name
dna methyltransferase 3 like protein (dnmt3l)
Structure deposition date
2007-05-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
8
% buried
26
Peptide accession
Q9UJW3
Residue number A
56
Residue number B
73
Peptide name
DNA (cytosine-5)-methyltransferase 3-like

Ligandability

Cysteine 56 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 73 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3-like between cysteines 53 and 73.

Details

Redox score ?
72
PDB code
2pvc
Structure name
dnmt3l recognizes unmethylated histone h3 lysine 4
Structure deposition date
2007-05-09
Thiol separation (Å)
3
Half-sphere exposure sum ?
66
Minimum pKa ?
10
% buried
nan
Peptide accession
Q9UJW3
Residue number A
53
Residue number B
73
Peptide name
DNA (cytosine-5)-methyltransferase 3-like

Ligandability

Cysteine 53 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 73 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3-like between cysteines 53 and 56.

Details

Redox score ?
72
PDB code
2pv0
Structure name
dna methyltransferase 3 like protein (dnmt3l)
Structure deposition date
2007-05-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
72
Minimum pKa ?
8
% buried
nan
Peptide accession
Q9UJW3
Residue number A
53
Residue number B
56
Peptide name
DNA (cytosine-5)-methyltransferase 3-like

Ligandability

Cysteine 53 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 56 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3-like between cysteines 108 and 145.

Details

Redox score ?
71
PDB code
2pvc
Structure name
dnmt3l recognizes unmethylated histone h3 lysine 4
Structure deposition date
2007-05-09
Thiol separation (Å)
3
Half-sphere exposure sum ?
55
Minimum pKa ?
13
% buried
57
Peptide accession
Q9UJW3
Residue number A
108
Residue number B
145
Peptide name
DNA (cytosine-5)-methyltransferase 3-like

Ligandability

Cysteine 108 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 145 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3-like between cysteines 53 and 76.

Details

Redox score ?
71
PDB code
2pvc
Structure name
dnmt3l recognizes unmethylated histone h3 lysine 4
Structure deposition date
2007-05-09
Thiol separation (Å)
3
Half-sphere exposure sum ?
72
Minimum pKa ?
11
% buried
nan
Peptide accession
Q9UJW3
Residue number A
53
Residue number B
76
Peptide name
DNA (cytosine-5)-methyltransferase 3-like

Ligandability

Cysteine 53 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 76 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3-like between cysteines 55 and 76.

Details

Redox score ?
68
PDB code
2pvc
Structure name
dnmt3l recognizes unmethylated histone h3 lysine 4
Structure deposition date
2007-05-09
Thiol separation (Å)
3
Half-sphere exposure sum ?
79
Minimum pKa ?
11
% buried
65
Peptide accession
Q9UJW3
Residue number A
55
Residue number B
76
Peptide name
DNA (cytosine-5)-methyltransferase 3-like

Ligandability

Cysteine 55 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 76 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3-like between cysteines 142 and 145.

Details

Redox score ?
67
PDB code
2pvc
Structure name
dnmt3l recognizes unmethylated histone h3 lysine 4
Structure deposition date
2007-05-09
Thiol separation (Å)
3
Half-sphere exposure sum ?
62
Minimum pKa ?
14
% buried
72
Peptide accession
Q9UJW3
Residue number A
142
Residue number B
145
Peptide name
DNA (cytosine-5)-methyltransferase 3-like

Ligandability

Cysteine 142 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 145 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3-like between cysteines 113 and 145.

Details

Redox score ?
65
PDB code
2pv0
Structure name
dna methyltransferase 3 like protein (dnmt3l)
Structure deposition date
2007-05-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
14
% buried
67
Peptide accession
Q9UJW3
Residue number A
113
Residue number B
145
Peptide name
DNA (cytosine-5)-methyltransferase 3-like

Ligandability

Cysteine 113 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 145 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3-like between cysteines 96 and 121.

Details

Redox score ?
61
PDB code
2pv0
Structure name
dna methyltransferase 3 like protein (dnmt3l)
Structure deposition date
2007-05-09
Thiol separation (Å)
3
Half-sphere exposure sum ?
73
Minimum pKa ?
14
% buried
94
Peptide accession
Q9UJW3
Residue number A
96
Residue number B
121
Peptide name
DNA (cytosine-5)-methyltransferase 3-like

Ligandability

Cysteine 96 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 121 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3-like between cysteines 96 and 118. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
2pvc
Structure name
dnmt3l recognizes unmethylated histone h3 lysine 4
Structure deposition date
2007-05-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
81
Minimum pKa ?
14
% buried
nan
Peptide accession
Q9UJW3
Residue number A
96
Residue number B
118
Peptide name
DNA (cytosine-5)-methyltransferase 3-like

Ligandability

Cysteine 96 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 118 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3-like between cysteines 96 and 99. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
2pvc
Structure name
dnmt3l recognizes unmethylated histone h3 lysine 4
Structure deposition date
2007-05-09
Thiol separation (Å)
3
Half-sphere exposure sum ?
83
Minimum pKa ?
16
% buried
nan
Peptide accession
Q9UJW3
Residue number A
96
Residue number B
99
Peptide name
DNA (cytosine-5)-methyltransferase 3-like

Ligandability

Cysteine 96 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 99 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3-like between cysteines 55 and 56. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
2pv0
Structure name
dna methyltransferase 3 like protein (dnmt3l)
Structure deposition date
2007-05-09
Thiol separation (Å)
6
Half-sphere exposure sum ?
83
Minimum pKa ?
10
% buried
40
Peptide accession
Q9UJW3
Residue number A
55
Residue number B
56
Peptide name
DNA (cytosine-5)-methyltransferase 3-like

Ligandability

Cysteine 55 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 56 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3-like between cysteines 76 and 99. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
2pvc
Structure name
dnmt3l recognizes unmethylated histone h3 lysine 4
Structure deposition date
2007-05-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
5
% buried
70
Peptide accession
Q9UJW3
Residue number A
76
Residue number B
99
Peptide name
DNA (cytosine-5)-methyltransferase 3-like

Ligandability

Cysteine 76 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 99 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3-like between cysteines 99 and 100. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
2pv0
Structure name
dna methyltransferase 3 like protein (dnmt3l)
Structure deposition date
2007-05-09
Thiol separation (Å)
6
Half-sphere exposure sum ?
77
Minimum pKa ?
12
% buried
nan
Peptide accession
Q9UJW3
Residue number A
99
Residue number B
100
Peptide name
DNA (cytosine-5)-methyltransferase 3-like

Ligandability

Cysteine 99 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 100 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3-like between cysteines 53 and 121. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
2pv0
Structure name
dna methyltransferase 3 like protein (dnmt3l)
Structure deposition date
2007-05-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
79
Minimum pKa ?
3
% buried
78
Peptide accession
Q9UJW3
Residue number A
53
Residue number B
121
Peptide name
DNA (cytosine-5)-methyltransferase 3-like

Ligandability

Cysteine 53 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 121 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3-like between cysteines 55 and 100. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
2pv0
Structure name
dna methyltransferase 3 like protein (dnmt3l)
Structure deposition date
2007-05-09
Thiol separation (Å)
6
Half-sphere exposure sum ?
84
Minimum pKa ?
12
% buried
89
Peptide accession
Q9UJW3
Residue number A
55
Residue number B
100
Peptide name
DNA (cytosine-5)-methyltransferase 3-like

Ligandability

Cysteine 55 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 100 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3-like between cysteines 96 and 100. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
2pv0
Structure name
dna methyltransferase 3 like protein (dnmt3l)
Structure deposition date
2007-05-09
Thiol separation (Å)
7
Half-sphere exposure sum ?
70
Minimum pKa ?
12
% buried
nan
Peptide accession
Q9UJW3
Residue number A
96
Residue number B
100
Peptide name
DNA (cytosine-5)-methyltransferase 3-like

Ligandability

Cysteine 96 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 100 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3-like between cysteines 100 and 118. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
2pv0
Structure name
dna methyltransferase 3 like protein (dnmt3l)
Structure deposition date
2007-05-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
74
Minimum pKa ?
5
% buried
77
Peptide accession
Q9UJW3
Residue number A
100
Residue number B
118
Peptide name
DNA (cytosine-5)-methyltransferase 3-like

Ligandability

Cysteine 100 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 118 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3-like between cysteines 108 and 142. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
2pvc
Structure name
dnmt3l recognizes unmethylated histone h3 lysine 4
Structure deposition date
2007-05-09
Thiol separation (Å)
3
Half-sphere exposure sum ?
70
Minimum pKa ?
23
% buried
nan
Peptide accession
Q9UJW3
Residue number A
108
Residue number B
142
Peptide name
DNA (cytosine-5)-methyltransferase 3-like

Ligandability

Cysteine 108 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 142 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3-like between cysteines 55 and 73. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
2pv0
Structure name
dna methyltransferase 3 like protein (dnmt3l)
Structure deposition date
2007-05-09
Thiol separation (Å)
7
Half-sphere exposure sum ?
77
Minimum pKa ?
12
% buried
59
Peptide accession
Q9UJW3
Residue number A
55
Residue number B
73
Peptide name
DNA (cytosine-5)-methyltransferase 3-like

Ligandability

Cysteine 55 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 73 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3-like between cysteines 76 and 100. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
2pvc
Structure name
dnmt3l recognizes unmethylated histone h3 lysine 4
Structure deposition date
2007-05-09
Thiol separation (Å)
8
Half-sphere exposure sum ?
67
Minimum pKa ?
11
% buried
64
Peptide accession
Q9UJW3
Residue number A
76
Residue number B
100
Peptide name
DNA (cytosine-5)-methyltransferase 3-like

Ligandability

Cysteine 76 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 100 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3-like between cysteines 55 and 118. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
2pvc
Structure name
dnmt3l recognizes unmethylated histone h3 lysine 4
Structure deposition date
2007-05-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
85
Minimum pKa ?
6
% buried
84
Peptide accession
Q9UJW3
Residue number A
55
Residue number B
118
Peptide name
DNA (cytosine-5)-methyltransferase 3-like

Ligandability

Cysteine 55 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 118 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3-like between cysteines 113 and 116. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
2pv0
Structure name
dna methyltransferase 3 like protein (dnmt3l)
Structure deposition date
2007-05-09
Thiol separation (Å)
8
Half-sphere exposure sum ?
67
Minimum pKa ?
11
% buried
74
Peptide accession
Q9UJW3
Residue number A
113
Residue number B
116
Peptide name
DNA (cytosine-5)-methyltransferase 3-like

Ligandability

Cysteine 113 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 116 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3-like between cysteines 99 and 121. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
2pvc
Structure name
dnmt3l recognizes unmethylated histone h3 lysine 4
Structure deposition date
2007-05-09
Thiol separation (Å)
3
Half-sphere exposure sum ?
89
Minimum pKa ?
24
% buried
nan
Peptide accession
Q9UJW3
Residue number A
99
Residue number B
121
Peptide name
DNA (cytosine-5)-methyltransferase 3-like

Ligandability

Cysteine 99 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 121 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3-like between cysteines 53 and 55. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
2pvc
Structure name
dnmt3l recognizes unmethylated histone h3 lysine 4
Structure deposition date
2007-05-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
84
Minimum pKa ?
21
% buried
nan
Peptide accession
Q9UJW3
Residue number A
53
Residue number B
55
Peptide name
DNA (cytosine-5)-methyltransferase 3-like

Ligandability

Cysteine 53 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 55 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3-like between cysteines 53 and 99. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
2pvc
Structure name
dnmt3l recognizes unmethylated histone h3 lysine 4
Structure deposition date
2007-05-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UJW3
Residue number A
53
Residue number B
99
Peptide name
DNA (cytosine-5)-methyltransferase 3-like

Ligandability

Cysteine 53 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 99 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3-like between cysteines 96 and 116. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
2pv0
Structure name
dna methyltransferase 3 like protein (dnmt3l)
Structure deposition date
2007-05-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
74
Minimum pKa ?
12
% buried
nan
Peptide accession
Q9UJW3
Residue number A
96
Residue number B
116
Peptide name
DNA (cytosine-5)-methyltransferase 3-like

Ligandability

Cysteine 96 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 116 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3-like between cysteines 55 and 99. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
2pvc
Structure name
dnmt3l recognizes unmethylated histone h3 lysine 4
Structure deposition date
2007-05-09
Thiol separation (Å)
6
Half-sphere exposure sum ?
90
Minimum pKa ?
16
% buried
90
Peptide accession
Q9UJW3
Residue number A
55
Residue number B
99
Peptide name
DNA (cytosine-5)-methyltransferase 3-like

Ligandability

Cysteine 55 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 99 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3-like between cysteines 116 and 142. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
2pvc
Structure name
dnmt3l recognizes unmethylated histone h3 lysine 4
Structure deposition date
2007-05-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
12
% buried
nan
Peptide accession
Q9UJW3
Residue number A
116
Residue number B
142
Peptide name
DNA (cytosine-5)-methyltransferase 3-like

Ligandability

Cysteine 116 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 142 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3-like between cysteines 108 and 116. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
2pvc
Structure name
dnmt3l recognizes unmethylated histone h3 lysine 4
Structure deposition date
2007-05-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
12
% buried
nan
Peptide accession
Q9UJW3
Residue number A
108
Residue number B
116
Peptide name
DNA (cytosine-5)-methyltransferase 3-like

Ligandability

Cysteine 108 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 116 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3-like between cysteines 116 and 118. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
2pv0
Structure name
dna methyltransferase 3 like protein (dnmt3l)
Structure deposition date
2007-05-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
78
Minimum pKa ?
11
% buried
55
Peptide accession
Q9UJW3
Residue number A
116
Residue number B
118
Peptide name
DNA (cytosine-5)-methyltransferase 3-like

Ligandability

Cysteine 116 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 118 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3-like between cysteines 100 and 121. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
2pv0
Structure name
dna methyltransferase 3 like protein (dnmt3l)
Structure deposition date
2007-05-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
74
Minimum pKa ?
12
% buried
86
Peptide accession
Q9UJW3
Residue number A
100
Residue number B
121
Peptide name
DNA (cytosine-5)-methyltransferase 3-like

Ligandability

Cysteine 100 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 121 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3-like between cysteines 56 and 99. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
2pv0
Structure name
dna methyltransferase 3 like protein (dnmt3l)
Structure deposition date
2007-05-09
Thiol separation (Å)
10
Half-sphere exposure sum ?
76
Minimum pKa ?
10
% buried
nan
Peptide accession
Q9UJW3
Residue number A
56
Residue number B
99
Peptide name
DNA (cytosine-5)-methyltransferase 3-like

Ligandability

Cysteine 56 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 99 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3-like between cysteines 53 and 100. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
PDB code
2pvc
Structure name
dnmt3l recognizes unmethylated histone h3 lysine 4
Structure deposition date
2007-05-09
Thiol separation (Å)
10
Half-sphere exposure sum ?
74
Minimum pKa ?
12
% buried
nan
Peptide accession
Q9UJW3
Residue number A
53
Residue number B
100
Peptide name
DNA (cytosine-5)-methyltransferase 3-like

Ligandability

Cysteine 53 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 100 of DNA (cytosine-5)-methyltransferase 3-like

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

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