Transcriptional regulator ATRX
Intermolecular
Cysteine 1614 and cysteine 1614
Intramolecular
Cysteine 235 and cysteine 268
Cysteine 171 and cysteine 197
Cysteine 171 and cysteine 200
Cysteine 232 and cysteine 265
Cysteine 232 and cysteine 235
Cysteine 171 and cysteine 174
Cysteine 232 and cysteine 268
Cysteine 220 and cysteine 240 L
Cysteine 223 and cysteine 243 L
More...Cysteine 220 and cysteine 223 L
Cysteine 235 and cysteine 265
Cysteine 197 and cysteine 200
Cysteine 265 and cysteine 268
Cysteine 174 and cysteine 200
Cysteine 174 and cysteine 197
Cysteine 223 and cysteine 240 L
Cysteine 240 and cysteine 243
Cysteine 171 and cysteine 280
Cysteine 174 and cysteine 240
Cysteine 171 and cysteine 243
Cysteine 174 and cysteine 220 L
Cysteine 171 and cysteine 223 L
Cysteine 231 and cysteine 232 L
Cysteine 174 and cysteine 243
Cysteine 220 and cysteine 243 L
Cysteine 231 and cysteine 235 L
Cysteine 174 and cysteine 223 L
Cysteine 200 and cysteine 280
Cysteine 197 and cysteine 280
Cysteine 200 and cysteine 223 L
Cysteine 231 and cysteine 265 L
Cysteine 220 and cysteine 265 L
Cysteine 200 and cysteine 243
Cysteine 197 and cysteine 223 L
Cysteine 200 and cysteine 220 L
5y6o E 58 H 58
A redox-regulated disulphide may form between two units of Transcriptional regulator ATRX at cysteines 1614 and 1614 (58 and 58 respectively in this structure).
Details
Redox score ?
80
PDB code
5y6o
Structure name
crystal structure of daxx n-terminal four-helix bundle domain (4hb) in complex with atrx
Structure deposition date
2017-08-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
nan
Minimum pKa ?
8
% buried
nan
Peptide A name
Transcriptional regulator ATRX
Peptide B name
Transcriptional regulator ATRX
Peptide A accession
P46100
Peptide B accession
P46100
Peptide A residue number
1614
Peptide B residue number
1614
Ligandability
3qla A 235 A 268
A redox-regulated disulphide may form within Transcriptional regulator ATRX between cysteines 235 and 268.
Details
Redox score ?
86
PDB code
3qla
Structure name
hexagonal complex structure of atrx add bound to h3k9me3 peptide
Structure deposition date
2011-02-02
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
4
% buried
36
Peptide accession
P46100
Residue number A
235
Residue number B
268
Peptide name
Transcriptional regulator ATRX
Ligandability
Cysteine 235 of Transcriptional regulator ATRX
Cysteine 268 of Transcriptional regulator ATRX
4w5a E 11 E 37
A redox-regulated disulphide may form within Transcriptional regulator ATRX between cysteines 171 and 197 (11 and 37 respectively in this structure).
Details
Redox score ?
85
PDB code
4w5a
Structure name
complex structure of atrx add bound to h3k9me3s10ph peptide
Structure deposition date
2014-08-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
3
% buried
46
Peptide accession
P46100
Residue number A
171
Residue number B
197
Peptide name
Transcriptional regulator ATRX
Ligandability
Cysteine 171 of Transcriptional regulator ATRX
Cysteine 197 of Transcriptional regulator ATRX
4w5a E 11 E 40
A redox-regulated disulphide may form within Transcriptional regulator ATRX between cysteines 171 and 200 (11 and 40 respectively in this structure).
Details
Redox score ?
85
PDB code
4w5a
Structure name
complex structure of atrx add bound to h3k9me3s10ph peptide
Structure deposition date
2014-08-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
3
% buried
58
Peptide accession
P46100
Residue number A
171
Residue number B
200
Peptide name
Transcriptional regulator ATRX
Ligandability
Cysteine 171 of Transcriptional regulator ATRX
Cysteine 200 of Transcriptional regulator ATRX
3qln B 232 B 265
A redox-regulated disulphide may form within Transcriptional regulator ATRX between cysteines 232 and 265.
Details
Redox score ?
80
PDB code
3qln
Structure name
crystal structure of atrx add domain in free state
Structure deposition date
2011-02-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
7
% buried
46
Peptide accession
P46100
Residue number A
232
Residue number B
265
Peptide name
Transcriptional regulator ATRX
Ligandability
Cysteine 232 of Transcriptional regulator ATRX
Cysteine 265 of Transcriptional regulator ATRX
3qlc A 232 A 235
A redox-regulated disulphide may form within Transcriptional regulator ATRX between cysteines 232 and 235.
Details
Redox score ?
79
PDB code
3qlc
Structure name
complex structure of atrx add domain bound to unmodified h3 1-15 peptide
Structure deposition date
2011-02-02
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
6
% buried
35
Peptide accession
P46100
Residue number A
232
Residue number B
235
Peptide name
Transcriptional regulator ATRX
Ligandability
Cysteine 232 of Transcriptional regulator ATRX
Cysteine 235 of Transcriptional regulator ATRX
3qln B 171 B 174
A redox-regulated disulphide may form within Transcriptional regulator ATRX between cysteines 171 and 174.
Details
Redox score ?
78
PDB code
3qln
Structure name
crystal structure of atrx add domain in free state
Structure deposition date
2011-02-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
7
% buried
42
Peptide accession
P46100
Residue number A
171
Residue number B
174
Peptide name
Transcriptional regulator ATRX
Ligandability
Cysteine 171 of Transcriptional regulator ATRX
Cysteine 174 of Transcriptional regulator ATRX
3qln A 232 A 268
A redox-regulated disulphide may form within Transcriptional regulator ATRX between cysteines 232 and 268.
Details
Redox score ?
78
PDB code
3qln
Structure name
crystal structure of atrx add domain in free state
Structure deposition date
2011-02-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
8
% buried
46
Peptide accession
P46100
Residue number A
232
Residue number B
268
Peptide name
Transcriptional regulator ATRX
Ligandability
Cysteine 232 of Transcriptional regulator ATRX
Cysteine 268 of Transcriptional regulator ATRX
3ql9 A 220 A 240
A redox-regulated disulphide may form within Transcriptional regulator ATRX between cysteines 220 and 240.
Details
Redox score ?
77
PDB code
3ql9
Structure name
monoclinic complex structure of atrx add bound to histone h3k9me3 peptide
Structure deposition date
2011-02-02
Thiol separation (Å)
4
Half-sphere exposure sum ?
84
Minimum pKa ?
6
% buried
nan
Peptide accession
P46100
Residue number A
220
Residue number B
240
Peptide name
Transcriptional regulator ATRX
Ligandability
Cysteine 220 of Transcriptional regulator ATRX
Cysteine 240 of Transcriptional regulator ATRX
4w5a A 63 A 83
A redox-regulated disulphide may form within Transcriptional regulator ATRX between cysteines 223 and 243 (63 and 83 respectively in this structure).
Details
Redox score ?
77
PDB code
4w5a
Structure name
complex structure of atrx add bound to h3k9me3s10ph peptide
Structure deposition date
2014-08-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
77
Minimum pKa ?
5
% buried
99
Peptide accession
P46100
Residue number A
223
Residue number B
243
Peptide name
Transcriptional regulator ATRX
Ligandability
Cysteine 223 of Transcriptional regulator ATRX
Cysteine 243 of Transcriptional regulator ATRX
4w5a A 60 A 63
A redox-regulated disulphide may form within Transcriptional regulator ATRX between cysteines 220 and 223 (60 and 63 respectively in this structure).
Details
Redox score ?
76
PDB code
4w5a
Structure name
complex structure of atrx add bound to h3k9me3s10ph peptide
Structure deposition date
2014-08-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
86
Minimum pKa ?
5
% buried
99
Peptide accession
P46100
Residue number A
220
Residue number B
223
Peptide name
Transcriptional regulator ATRX
Ligandability
Cysteine 220 of Transcriptional regulator ATRX
Cysteine 223 of Transcriptional regulator ATRX
4w5a A 75 A 105
A redox-regulated disulphide may form within Transcriptional regulator ATRX between cysteines 235 and 265 (75 and 105 respectively in this structure).
Details
Redox score ?
76
PDB code
4w5a
Structure name
complex structure of atrx add bound to h3k9me3s10ph peptide
Structure deposition date
2014-08-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
81
Minimum pKa ?
5
% buried
95
Peptide accession
P46100
Residue number A
235
Residue number B
265
Peptide name
Transcriptional regulator ATRX
Ligandability
Cysteine 235 of Transcriptional regulator ATRX
Cysteine 265 of Transcriptional regulator ATRX
3qlc B 197 B 200
A redox-regulated disulphide may form within Transcriptional regulator ATRX between cysteines 197 and 200.
Details
Redox score ?
75
PDB code
3qlc
Structure name
complex structure of atrx add domain bound to unmodified h3 1-15 peptide
Structure deposition date
2011-02-02
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
8
% buried
43
Peptide accession
P46100
Residue number A
197
Residue number B
200
Peptide name
Transcriptional regulator ATRX
Ligandability
Cysteine 197 of Transcriptional regulator ATRX
Cysteine 200 of Transcriptional regulator ATRX
4w5a B 105 B 108
A redox-regulated disulphide may form within Transcriptional regulator ATRX between cysteines 265 and 268 (105 and 108 respectively in this structure).
Details
Redox score ?
74
PDB code
4w5a
Structure name
complex structure of atrx add bound to h3k9me3s10ph peptide
Structure deposition date
2014-08-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
10
% buried
33
Peptide accession
P46100
Residue number A
265
Residue number B
268
Peptide name
Transcriptional regulator ATRX
Ligandability
Cysteine 265 of Transcriptional regulator ATRX
Cysteine 268 of Transcriptional regulator ATRX
3ql9 A 174 A 200
A redox-regulated disulphide may form within Transcriptional regulator ATRX between cysteines 174 and 200.
Details
Redox score ?
73
PDB code
3ql9
Structure name
monoclinic complex structure of atrx add bound to histone h3k9me3 peptide
Structure deposition date
2011-02-02
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
9
% buried
46
Peptide accession
P46100
Residue number A
174
Residue number B
200
Peptide name
Transcriptional regulator ATRX
Ligandability
Cysteine 174 of Transcriptional regulator ATRX
Cysteine 200 of Transcriptional regulator ATRX
4w5a A 14 A 37
A redox-regulated disulphide may form within Transcriptional regulator ATRX between cysteines 174 and 197 (14 and 37 respectively in this structure).
Details
Redox score ?
73
PDB code
4w5a
Structure name
complex structure of atrx add bound to h3k9me3s10ph peptide
Structure deposition date
2014-08-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
77
Minimum pKa ?
5
% buried
89
Peptide accession
P46100
Residue number A
174
Residue number B
197
Peptide name
Transcriptional regulator ATRX
Ligandability
Cysteine 174 of Transcriptional regulator ATRX
Cysteine 197 of Transcriptional regulator ATRX
3ql9 A 223 A 240
A redox-regulated disulphide may form within Transcriptional regulator ATRX between cysteines 223 and 240.
Details
Redox score ?
73
PDB code
3ql9
Structure name
monoclinic complex structure of atrx add bound to histone h3k9me3 peptide
Structure deposition date
2011-02-02
Thiol separation (Å)
4
Half-sphere exposure sum ?
86
Minimum pKa ?
6
% buried
86
Peptide accession
P46100
Residue number A
223
Residue number B
240
Peptide name
Transcriptional regulator ATRX
Ligandability
Cysteine 223 of Transcriptional regulator ATRX
Cysteine 240 of Transcriptional regulator ATRX
3qla A 240 A 243
A redox-regulated disulphide may form within Transcriptional regulator ATRX between cysteines 240 and 243.
Details
Redox score ?
69
PDB code
3qla
Structure name
hexagonal complex structure of atrx add bound to h3k9me3 peptide
Structure deposition date
2011-02-02
Thiol separation (Å)
4
Half-sphere exposure sum ?
77
Minimum pKa ?
10
% buried
92
Peptide accession
P46100
Residue number A
240
Residue number B
243
Peptide name
Transcriptional regulator ATRX
Ligandability
Cysteine 240 of Transcriptional regulator ATRX
Cysteine 243 of Transcriptional regulator ATRX
3ql9 A 171 A 280
A redox-regulated disulphide may form within Transcriptional regulator ATRX between cysteines 171 and 280. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
57
PDB code
3ql9
Structure name
monoclinic complex structure of atrx add bound to histone h3k9me3 peptide
Structure deposition date
2011-02-02
Thiol separation (Å)
10
Half-sphere exposure sum ?
65
Minimum pKa ?
0
% buried
68
Peptide accession
P46100
Residue number A
171
Residue number B
280
Peptide name
Transcriptional regulator ATRX
Ligandability
Cysteine 171 of Transcriptional regulator ATRX
Cysteine 280 of Transcriptional regulator ATRX
2jm1 A 174 A 240
A redox-regulated disulphide may form within Transcriptional regulator ATRX between cysteines 174 and 240. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
52
PDB code
2jm1
Structure name
structures and chemical shift assignments for the add domain of the atrx protein
Structure deposition date
2006-09-13
Thiol separation (Å)
10
Half-sphere exposure sum ?
63
Minimum pKa ?
2
% buried
50
Peptide accession
P46100
Residue number A
174
Residue number B
240
Peptide name
Transcriptional regulator ATRX
Ligandability
Cysteine 174 of Transcriptional regulator ATRX
Cysteine 240 of Transcriptional regulator ATRX
3qln B 171 B 243
A redox-regulated disulphide may form within Transcriptional regulator ATRX between cysteines 171 and 243. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
3qln
Structure name
crystal structure of atrx add domain in free state
Structure deposition date
2011-02-03
Thiol separation (Å)
8
Half-sphere exposure sum ?
68
Minimum pKa ?
7
% buried
66
Peptide accession
P46100
Residue number A
171
Residue number B
243
Peptide name
Transcriptional regulator ATRX
Ligandability
Cysteine 171 of Transcriptional regulator ATRX
Cysteine 243 of Transcriptional regulator ATRX
2jm1 A 174 A 220
A redox-regulated disulphide may form within Transcriptional regulator ATRX between cysteines 174 and 220. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
2jm1
Structure name
structures and chemical shift assignments for the add domain of the atrx protein
Structure deposition date
2006-09-13
Thiol separation (Å)
10
Half-sphere exposure sum ?
66
Minimum pKa ?
1
% buried
64
Peptide accession
P46100
Residue number A
174
Residue number B
220
Peptide name
Transcriptional regulator ATRX
Ligandability
Cysteine 174 of Transcriptional regulator ATRX
Cysteine 220 of Transcriptional regulator ATRX
4w5a E 11 E 63
A redox-regulated disulphide may form within Transcriptional regulator ATRX between cysteines 171 and 223 (11 and 63 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
4w5a
Structure name
complex structure of atrx add bound to h3k9me3s10ph peptide
Structure deposition date
2014-08-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
75
Minimum pKa ?
3
% buried
76
Peptide accession
P46100
Residue number A
171
Residue number B
223
Peptide name
Transcriptional regulator ATRX
Ligandability
Cysteine 171 of Transcriptional regulator ATRX
Cysteine 223 of Transcriptional regulator ATRX
3qln B 231 B 232
A redox-regulated disulphide may form within Transcriptional regulator ATRX between cysteines 231 and 232. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
3qln
Structure name
crystal structure of atrx add domain in free state
Structure deposition date
2011-02-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
61
Minimum pKa ?
7
% buried
32
Peptide accession
P46100
Residue number A
231
Residue number B
232
Peptide name
Transcriptional regulator ATRX
Ligandability
Cysteine 231 of Transcriptional regulator ATRX
Cysteine 232 of Transcriptional regulator ATRX
3qla A 174 A 243
A redox-regulated disulphide may form within Transcriptional regulator ATRX between cysteines 174 and 243. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
3qla
Structure name
hexagonal complex structure of atrx add bound to h3k9me3 peptide
Structure deposition date
2011-02-02
Thiol separation (Å)
9
Half-sphere exposure sum ?
70
Minimum pKa ?
5
% buried
72
Peptide accession
P46100
Residue number A
174
Residue number B
243
Peptide name
Transcriptional regulator ATRX
Ligandability
Cysteine 174 of Transcriptional regulator ATRX
Cysteine 243 of Transcriptional regulator ATRX
3ql9 A 220 A 243
A redox-regulated disulphide may form within Transcriptional regulator ATRX between cysteines 220 and 243. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
3ql9
Structure name
monoclinic complex structure of atrx add bound to histone h3k9me3 peptide
Structure deposition date
2011-02-02
Thiol separation (Å)
4
Half-sphere exposure sum ?
77
Minimum pKa ?
24
% buried
nan
Peptide accession
P46100
Residue number A
220
Residue number B
243
Peptide name
Transcriptional regulator ATRX
Ligandability
Cysteine 220 of Transcriptional regulator ATRX
Cysteine 243 of Transcriptional regulator ATRX
4w5a A 71 A 75
A redox-regulated disulphide may form within Transcriptional regulator ATRX between cysteines 231 and 235 (71 and 75 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
4w5a
Structure name
complex structure of atrx add bound to h3k9me3s10ph peptide
Structure deposition date
2014-08-17
Thiol separation (Å)
10
Half-sphere exposure sum ?
81
Minimum pKa ?
5
% buried
76
Peptide accession
P46100
Residue number A
231
Residue number B
235
Peptide name
Transcriptional regulator ATRX
Ligandability
Cysteine 231 of Transcriptional regulator ATRX
Cysteine 235 of Transcriptional regulator ATRX
4w5a E 14 E 63
A redox-regulated disulphide may form within Transcriptional regulator ATRX between cysteines 174 and 223 (14 and 63 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
4w5a
Structure name
complex structure of atrx add bound to h3k9me3s10ph peptide
Structure deposition date
2014-08-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
10
% buried
58
Peptide accession
P46100
Residue number A
174
Residue number B
223
Peptide name
Transcriptional regulator ATRX
Ligandability
Cysteine 174 of Transcriptional regulator ATRX
Cysteine 223 of Transcriptional regulator ATRX
2jm1 A 200 A 280
A redox-regulated disulphide may form within Transcriptional regulator ATRX between cysteines 200 and 280. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
36
PDB code
2jm1
Structure name
structures and chemical shift assignments for the add domain of the atrx protein
Structure deposition date
2006-09-13
Thiol separation (Å)
10
Half-sphere exposure sum ?
65
Minimum pKa ?
11
% buried
52
Peptide accession
P46100
Residue number A
200
Residue number B
280
Peptide name
Transcriptional regulator ATRX
Ligandability
Cysteine 200 of Transcriptional regulator ATRX
Cysteine 280 of Transcriptional regulator ATRX
2jm1 A 197 A 280
A redox-regulated disulphide may form within Transcriptional regulator ATRX between cysteines 197 and 280. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
35
PDB code
2jm1
Structure name
structures and chemical shift assignments for the add domain of the atrx protein
Structure deposition date
2006-09-13
Thiol separation (Å)
10
Half-sphere exposure sum ?
66
Minimum pKa ?
11
% buried
nan
Peptide accession
P46100
Residue number A
197
Residue number B
280
Peptide name
Transcriptional regulator ATRX
Ligandability
Cysteine 197 of Transcriptional regulator ATRX
Cysteine 280 of Transcriptional regulator ATRX
3ql9 A 200 A 223
A redox-regulated disulphide may form within Transcriptional regulator ATRX between cysteines 200 and 223. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
3ql9
Structure name
monoclinic complex structure of atrx add bound to histone h3k9me3 peptide
Structure deposition date
2011-02-02
Thiol separation (Å)
8
Half-sphere exposure sum ?
77
Minimum pKa ?
14
% buried
74
Peptide accession
P46100
Residue number A
200
Residue number B
223
Peptide name
Transcriptional regulator ATRX
Ligandability
Cysteine 200 of Transcriptional regulator ATRX
Cysteine 223 of Transcriptional regulator ATRX
3qla A 231 A 265
A redox-regulated disulphide may form within Transcriptional regulator ATRX between cysteines 231 and 265. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
33
PDB code
3qla
Structure name
hexagonal complex structure of atrx add bound to h3k9me3 peptide
Structure deposition date
2011-02-02
Thiol separation (Å)
10
Half-sphere exposure sum ?
76
Minimum pKa ?
11
% buried
64
Peptide accession
P46100
Residue number A
231
Residue number B
265
Peptide name
Transcriptional regulator ATRX
Ligandability
Cysteine 231 of Transcriptional regulator ATRX
Cysteine 265 of Transcriptional regulator ATRX
2ld1 A 220 A 265
A redox-regulated disulphide may form within Transcriptional regulator ATRX between cysteines 220 and 265. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
31
PDB code
2ld1
Structure name
structures and chemical shift assignments for the add domain of the atrx protein
Structure deposition date
2011-05-13
Thiol separation (Å)
10
Half-sphere exposure sum ?
71
Minimum pKa ?
12
% buried
nan
Peptide accession
P46100
Residue number A
220
Residue number B
265
Peptide name
Transcriptional regulator ATRX
Ligandability
Cysteine 220 of Transcriptional regulator ATRX
Cysteine 265 of Transcriptional regulator ATRX
3qlc A 200 A 243
A redox-regulated disulphide may form within Transcriptional regulator ATRX between cysteines 200 and 243. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
30
PDB code
3qlc
Structure name
complex structure of atrx add domain bound to unmodified h3 1-15 peptide
Structure deposition date
2011-02-02
Thiol separation (Å)
8
Half-sphere exposure sum ?
67
Minimum pKa ?
16
% buried
74
Peptide accession
P46100
Residue number A
200
Residue number B
243
Peptide name
Transcriptional regulator ATRX
Ligandability
Cysteine 200 of Transcriptional regulator ATRX
Cysteine 243 of Transcriptional regulator ATRX
2jm1 A 197 A 223
A redox-regulated disulphide may form within Transcriptional regulator ATRX between cysteines 197 and 223. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
23
PDB code
2jm1
Structure name
structures and chemical shift assignments for the add domain of the atrx protein
Structure deposition date
2006-09-13
Thiol separation (Å)
10
Half-sphere exposure sum ?
73
Minimum pKa ?
15
% buried
nan
Peptide accession
P46100
Residue number A
197
Residue number B
223
Peptide name
Transcriptional regulator ATRX
Ligandability
Cysteine 197 of Transcriptional regulator ATRX
Cysteine 223 of Transcriptional regulator ATRX
3qla D 200 D 220
A redox-regulated disulphide may form within Transcriptional regulator ATRX between cysteines 200 and 220. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
14
PDB code
3qla
Structure name
hexagonal complex structure of atrx add bound to h3k9me3 peptide
Structure deposition date
2011-02-02
Thiol separation (Å)
10
Half-sphere exposure sum ?
79
Minimum pKa ?
20
% buried
nan
Peptide accession
P46100
Residue number A
200
Residue number B
220
Peptide name
Transcriptional regulator ATRX
Ligandability
Cysteine 200 of Transcriptional regulator ATRX
Cysteine 220 of Transcriptional regulator ATRX
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