Metal-response element-binding transcription factor 2
Intramolecular
Cysteine 122 and cysteine 125 L
Cysteine 122 and cysteine 154
Cysteine 122 and cysteine 151
Cysteine 125 and cysteine 154 L
Cysteine 204 and cysteine 206
Cysteine 108 and cysteine 133
Cysteine 105 and cysteine 108
Cysteine 222 and cysteine 252
Cysteine 125 and cysteine 151 L
Cysteine 249 and cysteine 252
More...Cysteine 219 and cysteine 252
Cysteine 204 and cysteine 230
Cysteine 151 and cysteine 154
Cysteine 219 and cysteine 222
Cysteine 222 and cysteine 249
Cysteine 219 and cysteine 220
Cysteine 44 and cysteine 76
Cysteine 105 and cysteine 133
Cysteine 219 and cysteine 249
Cysteine 220 and cysteine 252
Cysteine 206 and cysteine 230
Cysteine 204 and cysteine 249
Cysteine 220 and cysteine 222
Cysteine 202 and cysteine 204
Cysteine 202 and cysteine 206
Cysteine 220 and cysteine 249
5xfr A 122 A 125
A redox-regulated disulphide may form within Metal-response element-binding transcription factor 2 between cysteines 122 and 125.
Details
Redox score ?
85
PDB code
5xfr
Structure name
ternary complex of mtf2, dna and histone
Structure deposition date
2017-04-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
6
% buried
29
Peptide accession
Q9Y483
Residue number A
122
Residue number B
125
Peptide name
Metal-response element-binding transcription factor 2
Ligandability
Cysteine 122 of Metal-response element-binding transcription factor 2
Cysteine 125 of Metal-response element-binding transcription factor 2
5xfr B 122 B 154
A redox-regulated disulphide may form within Metal-response element-binding transcription factor 2 between cysteines 122 and 154.
Details
Redox score ?
85
PDB code
5xfr
Structure name
ternary complex of mtf2, dna and histone
Structure deposition date
2017-04-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
6
% buried
23
Peptide accession
Q9Y483
Residue number A
122
Residue number B
154
Peptide name
Metal-response element-binding transcription factor 2
Ligandability
Cysteine 122 of Metal-response element-binding transcription factor 2
Cysteine 154 of Metal-response element-binding transcription factor 2
5xfr A 122 A 151
A redox-regulated disulphide may form within Metal-response element-binding transcription factor 2 between cysteines 122 and 151.
Details
Redox score ?
82
PDB code
5xfr
Structure name
ternary complex of mtf2, dna and histone
Structure deposition date
2017-04-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
6
% buried
48
Peptide accession
Q9Y483
Residue number A
122
Residue number B
151
Peptide name
Metal-response element-binding transcription factor 2
Ligandability
Cysteine 122 of Metal-response element-binding transcription factor 2
Cysteine 151 of Metal-response element-binding transcription factor 2
5xfr B 125 B 154
A redox-regulated disulphide may form within Metal-response element-binding transcription factor 2 between cysteines 125 and 154.
Details
Redox score ?
80
PDB code
5xfr
Structure name
ternary complex of mtf2, dna and histone
Structure deposition date
2017-04-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
44
Minimum pKa ?
8
% buried
18
Peptide accession
Q9Y483
Residue number A
125
Residue number B
154
Peptide name
Metal-response element-binding transcription factor 2
Ligandability
Cysteine 125 of Metal-response element-binding transcription factor 2
Cysteine 154 of Metal-response element-binding transcription factor 2
5xfr B 204 B 206
A redox-regulated disulphide may form within Metal-response element-binding transcription factor 2 between cysteines 204 and 206.
Details
Redox score ?
77
PDB code
5xfr
Structure name
ternary complex of mtf2, dna and histone
Structure deposition date
2017-04-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
88
Minimum pKa ?
6
% buried
nan
Peptide accession
Q9Y483
Residue number A
204
Residue number B
206
Peptide name
Metal-response element-binding transcription factor 2
Ligandability
Cysteine 204 of Metal-response element-binding transcription factor 2
Cysteine 206 of Metal-response element-binding transcription factor 2
5xfr B 108 B 133
A redox-regulated disulphide may form within Metal-response element-binding transcription factor 2 between cysteines 108 and 133.
Details
Redox score ?
77
PDB code
5xfr
Structure name
ternary complex of mtf2, dna and histone
Structure deposition date
2017-04-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
43
Minimum pKa ?
9
% buried
0
Peptide accession
Q9Y483
Residue number A
108
Residue number B
133
Peptide name
Metal-response element-binding transcription factor 2
Ligandability
Cysteine 108 of Metal-response element-binding transcription factor 2
Cysteine 133 of Metal-response element-binding transcription factor 2
5xfr A 105 A 108
A redox-regulated disulphide may form within Metal-response element-binding transcription factor 2 between cysteines 105 and 108.
Details
Redox score ?
76
PDB code
5xfr
Structure name
ternary complex of mtf2, dna and histone
Structure deposition date
2017-04-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
10
% buried
nan
Peptide accession
Q9Y483
Residue number A
105
Residue number B
108
Peptide name
Metal-response element-binding transcription factor 2
Ligandability
Cysteine 105 of Metal-response element-binding transcription factor 2
Cysteine 108 of Metal-response element-binding transcription factor 2
5xfr B 222 B 252
A redox-regulated disulphide may form within Metal-response element-binding transcription factor 2 between cysteines 222 and 252.
Details
Redox score ?
76
PDB code
5xfr
Structure name
ternary complex of mtf2, dna and histone
Structure deposition date
2017-04-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
43
Minimum pKa ?
9
% buried
46
Peptide accession
Q9Y483
Residue number A
222
Residue number B
252
Peptide name
Metal-response element-binding transcription factor 2
Ligandability
Cysteine 222 of Metal-response element-binding transcription factor 2
Cysteine 252 of Metal-response element-binding transcription factor 2
5xfr A 125 A 151
A redox-regulated disulphide may form within Metal-response element-binding transcription factor 2 between cysteines 125 and 151.
Details
Redox score ?
76
PDB code
5xfr
Structure name
ternary complex of mtf2, dna and histone
Structure deposition date
2017-04-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
8
% buried
40
Peptide accession
Q9Y483
Residue number A
125
Residue number B
151
Peptide name
Metal-response element-binding transcription factor 2
Ligandability
Cysteine 125 of Metal-response element-binding transcription factor 2
Cysteine 151 of Metal-response element-binding transcription factor 2
5xfr B 249 B 252
A redox-regulated disulphide may form within Metal-response element-binding transcription factor 2 between cysteines 249 and 252.
Details
Redox score ?
76
PDB code
5xfr
Structure name
ternary complex of mtf2, dna and histone
Structure deposition date
2017-04-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
9
% buried
45
Peptide accession
Q9Y483
Residue number A
249
Residue number B
252
Peptide name
Metal-response element-binding transcription factor 2
Ligandability
Cysteine 249 of Metal-response element-binding transcription factor 2
Cysteine 252 of Metal-response element-binding transcription factor 2
5xfr B 219 B 252
A redox-regulated disulphide may form within Metal-response element-binding transcription factor 2 between cysteines 219 and 252.
Details
Redox score ?
75
PDB code
5xfr
Structure name
ternary complex of mtf2, dna and histone
Structure deposition date
2017-04-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
9
% buried
nan
Peptide accession
Q9Y483
Residue number A
219
Residue number B
252
Peptide name
Metal-response element-binding transcription factor 2
Ligandability
Cysteine 219 of Metal-response element-binding transcription factor 2
Cysteine 252 of Metal-response element-binding transcription factor 2
5xfr A 204 A 230
A redox-regulated disulphide may form within Metal-response element-binding transcription factor 2 between cysteines 204 and 230.
Details
Redox score ?
74
PDB code
5xfr
Structure name
ternary complex of mtf2, dna and histone
Structure deposition date
2017-04-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
89
Minimum pKa ?
6
% buried
100
Peptide accession
Q9Y483
Residue number A
204
Residue number B
230
Peptide name
Metal-response element-binding transcription factor 2
Ligandability
Cysteine 204 of Metal-response element-binding transcription factor 2
Cysteine 230 of Metal-response element-binding transcription factor 2
5xfr A 151 A 154
A redox-regulated disulphide may form within Metal-response element-binding transcription factor 2 between cysteines 151 and 154.
Details
Redox score ?
72
PDB code
5xfr
Structure name
ternary complex of mtf2, dna and histone
Structure deposition date
2017-04-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
10
% buried
46
Peptide accession
Q9Y483
Residue number A
151
Residue number B
154
Peptide name
Metal-response element-binding transcription factor 2
Ligandability
Cysteine 151 of Metal-response element-binding transcription factor 2
Cysteine 154 of Metal-response element-binding transcription factor 2
5xfr B 219 B 222
A redox-regulated disulphide may form within Metal-response element-binding transcription factor 2 between cysteines 219 and 222.
Details
Redox score ?
72
PDB code
5xfr
Structure name
ternary complex of mtf2, dna and histone
Structure deposition date
2017-04-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
11
% buried
nan
Peptide accession
Q9Y483
Residue number A
219
Residue number B
222
Peptide name
Metal-response element-binding transcription factor 2
Ligandability
Cysteine 219 of Metal-response element-binding transcription factor 2
Cysteine 222 of Metal-response element-binding transcription factor 2
5xfr B 222 B 249
A redox-regulated disulphide may form within Metal-response element-binding transcription factor 2 between cysteines 222 and 249.
Details
Redox score ?
70
PDB code
5xfr
Structure name
ternary complex of mtf2, dna and histone
Structure deposition date
2017-04-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
11
% buried
63
Peptide accession
Q9Y483
Residue number A
222
Residue number B
249
Peptide name
Metal-response element-binding transcription factor 2
Ligandability
Cysteine 222 of Metal-response element-binding transcription factor 2
Cysteine 249 of Metal-response element-binding transcription factor 2
5xfr A 219 A 220
A redox-regulated disulphide may form within Metal-response element-binding transcription factor 2 between cysteines 219 and 220.
Details
Redox score ?
63
PDB code
5xfr
Structure name
ternary complex of mtf2, dna and histone
Structure deposition date
2017-04-11
Thiol separation (Å)
5
Half-sphere exposure sum ?
63
Minimum pKa ?
10
% buried
nan
Peptide accession
Q9Y483
Residue number A
219
Residue number B
220
Peptide name
Metal-response element-binding transcription factor 2
Ligandability
Cysteine 219 of Metal-response element-binding transcription factor 2
Cysteine 220 of Metal-response element-binding transcription factor 2
2eqj A 12 A 44
A redox-regulated disulphide may form within Metal-response element-binding transcription factor 2 between cysteines 44 and 76 (12 and 44 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
55
PDB code
2eqj
Structure name
solution structure of the tudor domain of metal-response element- binding transcription factor 2
Structure deposition date
2007-03-30
Thiol separation (Å)
8
Half-sphere exposure sum ?
55
Minimum pKa ?
9
% buried
18
Peptide accession
Q02395
Residue number A
44
Residue number B
76
Peptide name
Metal-response element-binding transcription factor 2
Ligandability
Cysteine 44 of Metal-response element-binding transcription factor 2
Cysteine 76 of Metal-response element-binding transcription factor 2
5xfr A 105 A 133
A redox-regulated disulphide may form within Metal-response element-binding transcription factor 2 between cysteines 105 and 133. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
55
PDB code
5xfr
Structure name
ternary complex of mtf2, dna and histone
Structure deposition date
2017-04-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
18
% buried
nan
Peptide accession
Q9Y483
Residue number A
105
Residue number B
133
Peptide name
Metal-response element-binding transcription factor 2
Ligandability
Cysteine 105 of Metal-response element-binding transcription factor 2
Cysteine 133 of Metal-response element-binding transcription factor 2
5xfr B 219 B 249
A redox-regulated disulphide may form within Metal-response element-binding transcription factor 2 between cysteines 219 and 249. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
52
PDB code
5xfr
Structure name
ternary complex of mtf2, dna and histone
Structure deposition date
2017-04-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
19
% buried
nan
Peptide accession
Q9Y483
Residue number A
219
Residue number B
249
Peptide name
Metal-response element-binding transcription factor 2
Ligandability
Cysteine 219 of Metal-response element-binding transcription factor 2
Cysteine 249 of Metal-response element-binding transcription factor 2
5xfr B 220 B 252
A redox-regulated disulphide may form within Metal-response element-binding transcription factor 2 between cysteines 220 and 252. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
52
PDB code
5xfr
Structure name
ternary complex of mtf2, dna and histone
Structure deposition date
2017-04-11
Thiol separation (Å)
8
Half-sphere exposure sum ?
49
Minimum pKa ?
9
% buried
21
Peptide accession
Q9Y483
Residue number A
220
Residue number B
252
Peptide name
Metal-response element-binding transcription factor 2
Ligandability
Cysteine 220 of Metal-response element-binding transcription factor 2
Cysteine 252 of Metal-response element-binding transcription factor 2
5xfr B 206 B 230
A redox-regulated disulphide may form within Metal-response element-binding transcription factor 2 between cysteines 206 and 230. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
5xfr
Structure name
ternary complex of mtf2, dna and histone
Structure deposition date
2017-04-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
89
Minimum pKa ?
19
% buried
nan
Peptide accession
Q9Y483
Residue number A
206
Residue number B
230
Peptide name
Metal-response element-binding transcription factor 2
Ligandability
Cysteine 206 of Metal-response element-binding transcription factor 2
Cysteine 230 of Metal-response element-binding transcription factor 2
5xfr A 204 A 249
A redox-regulated disulphide may form within Metal-response element-binding transcription factor 2 between cysteines 204 and 249. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
5xfr
Structure name
ternary complex of mtf2, dna and histone
Structure deposition date
2017-04-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
83
Minimum pKa ?
6
% buried
86
Peptide accession
Q9Y483
Residue number A
204
Residue number B
249
Peptide name
Metal-response element-binding transcription factor 2
Ligandability
Cysteine 204 of Metal-response element-binding transcription factor 2
Cysteine 249 of Metal-response element-binding transcription factor 2
5xfr B 220 B 222
A redox-regulated disulphide may form within Metal-response element-binding transcription factor 2 between cysteines 220 and 222. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
5xfr
Structure name
ternary complex of mtf2, dna and histone
Structure deposition date
2017-04-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
48
Minimum pKa ?
9
% buried
39
Peptide accession
Q9Y483
Residue number A
220
Residue number B
222
Peptide name
Metal-response element-binding transcription factor 2
Ligandability
Cysteine 220 of Metal-response element-binding transcription factor 2
Cysteine 222 of Metal-response element-binding transcription factor 2
5xfr B 202 B 204
A redox-regulated disulphide may form within Metal-response element-binding transcription factor 2 between cysteines 202 and 204. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
5xfr
Structure name
ternary complex of mtf2, dna and histone
Structure deposition date
2017-04-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
83
Minimum pKa ?
6
% buried
81
Peptide accession
Q9Y483
Residue number A
202
Residue number B
204
Peptide name
Metal-response element-binding transcription factor 2
Ligandability
Cysteine 202 of Metal-response element-binding transcription factor 2
Cysteine 204 of Metal-response element-binding transcription factor 2
5xfr B 202 B 206
A redox-regulated disulphide may form within Metal-response element-binding transcription factor 2 between cysteines 202 and 206. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
5xfr
Structure name
ternary complex of mtf2, dna and histone
Structure deposition date
2017-04-11
Thiol separation (Å)
8
Half-sphere exposure sum ?
83
Minimum pKa ?
11
% buried
nan
Peptide accession
Q9Y483
Residue number A
202
Residue number B
206
Peptide name
Metal-response element-binding transcription factor 2
Ligandability
Cysteine 202 of Metal-response element-binding transcription factor 2
Cysteine 206 of Metal-response element-binding transcription factor 2
5xfr A 220 A 249
A redox-regulated disulphide may form within Metal-response element-binding transcription factor 2 between cysteines 220 and 249. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
5xfr
Structure name
ternary complex of mtf2, dna and histone
Structure deposition date
2017-04-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
68
Minimum pKa ?
10
% buried
50
Peptide accession
Q9Y483
Residue number A
220
Residue number B
249
Peptide name
Metal-response element-binding transcription factor 2
Ligandability
Cysteine 220 of Metal-response element-binding transcription factor 2
Cysteine 249 of Metal-response element-binding transcription factor 2
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