Huntingtin
Intramolecular
Cysteine 1047 and cysteine 1062
Cysteine 103 and cysteine 135
Cysteine 772 and cysteine 807
Cysteine 107 and cysteine 150
Cysteine 3092 and cysteine 3132
Cysteine 838 and cysteine 1889
Cysteine 1358 and cysteine 1889
Cysteine 2833 and cysteine 2859
Cysteine 807 and cysteine 833
Cysteine 777 and cysteine 833
More...Cysteine 1998 and cysteine 2971 L
Cysteine 103 and cysteine 107
Cysteine 103 and cysteine 150
Cysteine 2108 and cysteine 2148
Cysteine 772 and cysteine 833
Cysteine 1025 and cysteine 1026
Cysteine 1708 and cysteine 1808 L
Cysteine 1961 and cysteine 1998
Cysteine 1152 and cysteine 1300
Cysteine 1903 and cysteine 1907
Cysteine 684 and cysteine 718
Cysteine 135 and cysteine 150
Cysteine 107 and cysteine 135
Cysteine 823 and cysteine 827 L
Cysteine 2281 and cysteine 2282
Cysteine 2282 and cysteine 2283
Cysteine 2833 and cysteine 2877
Cysteine 2305 and cysteine 2360
Cysteine 2859 and cysteine 2877
Cysteine 833 and cysteine 838
Cysteine 1026 and cysteine 1030
Cysteine 1300 and cysteine 1311
Cysteine 2282 and cysteine 2310
Cysteine 2281 and cysteine 2283
6x9o A 1049 A 1064
A redox-regulated disulphide may form within Huntingtin between cysteines 1047 and 1062 (1049 and 1064 respectively in this structure).
Details
Redox score ?
94
PDB code
6x9o
Structure name
high resolution cryoem structure of huntingtin in complex with hap40
Structure deposition date
2020-06-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P42858
Residue number A
1047
Residue number B
1062
Peptide name
Huntingtin
Ligandability
Cysteine 1047 of Huntingtin
Cysteine 1062 of Huntingtin
6x9o A 105 A 137
A redox-regulated disulphide may form within Huntingtin between cysteines 103 and 135 (105 and 137 respectively in this structure).
Details
Redox score ?
83
PDB code
6x9o
Structure name
high resolution cryoem structure of huntingtin in complex with hap40
Structure deposition date
2020-06-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P42858
Residue number A
103
Residue number B
135
Peptide name
Huntingtin
Ligandability
Cysteine 103 of Huntingtin
Cysteine 135 of Huntingtin
6rmh A 768 A 803
A redox-regulated disulphide may form within Huntingtin between cysteines 772 and 807 (768 and 803 respectively in this structure).
Details
Redox score ?
78
PDB code
6rmh
Structure name
the rigid-body refined model of the normal huntingtin
Structure deposition date
2019-05-06
Thiol separation (Å)
2
Half-sphere exposure sum ?
86
Minimum pKa ?
nan
% buried
nan
Peptide accession
P42858
Residue number A
772
Residue number B
807
Peptide name
Huntingtin
Ligandability
Cysteine 772 of Huntingtin
Cysteine 807 of Huntingtin
7dxj A 103 A 146
A redox-regulated disulphide may form within Huntingtin between cysteines 107 and 150 (103 and 146 respectively in this structure).
Details
Redox score ?
76
PDB code
7dxj
Structure name
human 46qhuntingtin-hap40 complex structure
Structure deposition date
2021-01-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
7
% buried
53
Peptide accession
P42858
Residue number A
107
Residue number B
150
Peptide name
Huntingtin
Ligandability
Cysteine 107 of Huntingtin
Cysteine 150 of Huntingtin
6x9o A 3094 A 3134
A redox-regulated disulphide may form within Huntingtin between cysteines 3092 and 3132 (3094 and 3134 respectively in this structure).
Details
Redox score ?
67
PDB code
6x9o
Structure name
high resolution cryoem structure of huntingtin in complex with hap40
Structure deposition date
2020-06-03
Thiol separation (Å)
5
Half-sphere exposure sum ?
63
Minimum pKa ?
10
% buried
46
Peptide accession
P42858
Residue number A
3092
Residue number B
3132
Peptide name
Huntingtin
Ligandability
Cysteine 3092 of Huntingtin
Cysteine 3132 of Huntingtin
6ez8 A 834 A 1885
A redox-regulated disulphide may form within Huntingtin between cysteines 838 and 1889 (834 and 1885 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
54
PDB code
6ez8
Structure name
human huntingtin-hap40 complex structure
Structure deposition date
2017-11-14
Thiol separation (Å)
5
Half-sphere exposure sum ?
79
Minimum pKa ?
12
% buried
92
Peptide accession
P42858
Residue number A
838
Residue number B
1889
Peptide name
Huntingtin
Ligandability
Cysteine 838 of Huntingtin
Cysteine 1889 of Huntingtin
6rmh A 1354 A 1885
A redox-regulated disulphide may form within Huntingtin between cysteines 1358 and 1889 (1354 and 1885 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
6rmh
Structure name
the rigid-body refined model of the normal huntingtin
Structure deposition date
2019-05-06
Thiol separation (Å)
8
Half-sphere exposure sum ?
63
Minimum pKa ?
11
% buried
50
Peptide accession
P42858
Residue number A
1358
Residue number B
1889
Peptide name
Huntingtin
Ligandability
Cysteine 1358 of Huntingtin
Cysteine 1889 of Huntingtin
7dxk A 2829 A 2855
A redox-regulated disulphide may form within Huntingtin between cysteines 2833 and 2859 (2829 and 2855 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
7dxk
Structure name
human 128qhuntingtin-hap40 complex structure
Structure deposition date
2021-01-19
Thiol separation (Å)
7
Half-sphere exposure sum ?
85
Minimum pKa ?
9
% buried
100
Peptide accession
P42858
Residue number A
2833
Residue number B
2859
Peptide name
Huntingtin
Ligandability
Cysteine 2833 of Huntingtin
Cysteine 2859 of Huntingtin
7dxk A 803 A 829
A redox-regulated disulphide may form within Huntingtin between cysteines 807 and 833 (803 and 829 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
7dxk
Structure name
human 128qhuntingtin-hap40 complex structure
Structure deposition date
2021-01-19
Thiol separation (Å)
7
Half-sphere exposure sum ?
74
Minimum pKa ?
13
% buried
nan
Peptide accession
P42858
Residue number A
807
Residue number B
833
Peptide name
Huntingtin
Ligandability
Cysteine 807 of Huntingtin
Cysteine 833 of Huntingtin
6rmh A 773 A 829
A redox-regulated disulphide may form within Huntingtin between cysteines 777 and 833 (773 and 829 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
6rmh
Structure name
the rigid-body refined model of the normal huntingtin
Structure deposition date
2019-05-06
Thiol separation (Å)
8
Half-sphere exposure sum ?
82
Minimum pKa ?
10
% buried
78
Peptide accession
P42858
Residue number A
777
Residue number B
833
Peptide name
Huntingtin
Ligandability
Cysteine 777 of Huntingtin
Cysteine 833 of Huntingtin
6rmh A 1994 A 2967
A redox-regulated disulphide may form within Huntingtin between cysteines 1998 and 2971 (1994 and 2967 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
6rmh
Structure name
the rigid-body refined model of the normal huntingtin
Structure deposition date
2019-05-06
Thiol separation (Å)
8
Half-sphere exposure sum ?
62
Minimum pKa ?
10
% buried
70
Peptide accession
P42858
Residue number A
1998
Residue number B
2971
Peptide name
Huntingtin
Ligandability
Cysteine 1998 of Huntingtin
Cysteine 2971 of Huntingtin
7dxj A 99 A 103
A redox-regulated disulphide may form within Huntingtin between cysteines 103 and 107 (99 and 103 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
7dxj
Structure name
human 46qhuntingtin-hap40 complex structure
Structure deposition date
2021-01-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
65
Minimum pKa ?
7
% buried
nan
Peptide accession
P42858
Residue number A
103
Residue number B
107
Peptide name
Huntingtin
Ligandability
Cysteine 103 of Huntingtin
Cysteine 107 of Huntingtin
7dxj A 99 A 146
A redox-regulated disulphide may form within Huntingtin between cysteines 103 and 150 (99 and 146 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
7dxj
Structure name
human 46qhuntingtin-hap40 complex structure
Structure deposition date
2021-01-19
Thiol separation (Å)
7
Half-sphere exposure sum ?
70
Minimum pKa ?
15
% buried
nan
Peptide accession
P42858
Residue number A
103
Residue number B
150
Peptide name
Huntingtin
Ligandability
Cysteine 103 of Huntingtin
Cysteine 150 of Huntingtin
6x9o A 2110 A 2150
A redox-regulated disulphide may form within Huntingtin between cysteines 2108 and 2148 (2110 and 2150 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
6x9o
Structure name
high resolution cryoem structure of huntingtin in complex with hap40
Structure deposition date
2020-06-03
Thiol separation (Å)
7
Half-sphere exposure sum ?
84
Minimum pKa ?
12
% buried
97
Peptide accession
P42858
Residue number A
2108
Residue number B
2148
Peptide name
Huntingtin
Ligandability
Cysteine 2108 of Huntingtin
Cysteine 2148 of Huntingtin
7dxj A 768 A 829
A redox-regulated disulphide may form within Huntingtin between cysteines 772 and 833 (768 and 829 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
7dxj
Structure name
human 46qhuntingtin-hap40 complex structure
Structure deposition date
2021-01-19
Thiol separation (Å)
7
Half-sphere exposure sum ?
96
Minimum pKa ?
13
% buried
nan
Peptide accession
P42858
Residue number A
772
Residue number B
833
Peptide name
Huntingtin
Ligandability
Cysteine 772 of Huntingtin
Cysteine 833 of Huntingtin
6ez8 A 1021 A 1022
A redox-regulated disulphide may form within Huntingtin between cysteines 1025 and 1026 (1021 and 1022 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
6ez8
Structure name
human huntingtin-hap40 complex structure
Structure deposition date
2017-11-14
Thiol separation (Å)
7
Half-sphere exposure sum ?
89
Minimum pKa ?
12
% buried
100
Peptide accession
P42858
Residue number A
1025
Residue number B
1026
Peptide name
Huntingtin
Ligandability
Cysteine 1025 of Huntingtin
Cysteine 1026 of Huntingtin
6x9o A 1710 A 1810
A redox-regulated disulphide may form within Huntingtin between cysteines 1708 and 1808 (1710 and 1810 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
6x9o
Structure name
high resolution cryoem structure of huntingtin in complex with hap40
Structure deposition date
2020-06-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
43
Minimum pKa ?
9
% buried
27
Peptide accession
P42858
Residue number A
1708
Residue number B
1808
Peptide name
Huntingtin
Ligandability
Cysteine 1708 of Huntingtin
Cysteine 1808 of Huntingtin
7dxj A 1957 A 1994
A redox-regulated disulphide may form within Huntingtin between cysteines 1961 and 1998 (1957 and 1994 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
7dxj
Structure name
human 46qhuntingtin-hap40 complex structure
Structure deposition date
2021-01-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
50
Minimum pKa ?
9
% buried
32
Peptide accession
P42858
Residue number A
1961
Residue number B
1998
Peptide name
Huntingtin
Ligandability
Cysteine 1961 of Huntingtin
Cysteine 1998 of Huntingtin
7dxk A 1148 A 1296
A redox-regulated disulphide may form within Huntingtin between cysteines 1152 and 1300 (1148 and 1296 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
7dxk
Structure name
human 128qhuntingtin-hap40 complex structure
Structure deposition date
2021-01-19
Thiol separation (Å)
7
Half-sphere exposure sum ?
81
Minimum pKa ?
12
% buried
95
Peptide accession
P42858
Residue number A
1152
Residue number B
1300
Peptide name
Huntingtin
Ligandability
Cysteine 1152 of Huntingtin
Cysteine 1300 of Huntingtin
6ez8 A 1899 A 1903
A redox-regulated disulphide may form within Huntingtin between cysteines 1903 and 1907 (1899 and 1903 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
6ez8
Structure name
human huntingtin-hap40 complex structure
Structure deposition date
2017-11-14
Thiol separation (Å)
9
Half-sphere exposure sum ?
67
Minimum pKa ?
10
% buried
62
Peptide accession
P42858
Residue number A
1903
Residue number B
1907
Peptide name
Huntingtin
Ligandability
Cysteine 1903 of Huntingtin
Cysteine 1907 of Huntingtin
7dxk A 680 A 714
A redox-regulated disulphide may form within Huntingtin between cysteines 684 and 718 (680 and 714 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
7dxk
Structure name
human 128qhuntingtin-hap40 complex structure
Structure deposition date
2021-01-19
Thiol separation (Å)
7
Half-sphere exposure sum ?
84
Minimum pKa ?
11
% buried
100
Peptide accession
P42858
Residue number A
684
Residue number B
718
Peptide name
Huntingtin
Ligandability
Cysteine 684 of Huntingtin
Cysteine 718 of Huntingtin
7dxj A 131 A 146
A redox-regulated disulphide may form within Huntingtin between cysteines 135 and 150 (131 and 146 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
7dxj
Structure name
human 46qhuntingtin-hap40 complex structure
Structure deposition date
2021-01-19
Thiol separation (Å)
7
Half-sphere exposure sum ?
74
Minimum pKa ?
15
% buried
nan
Peptide accession
P42858
Residue number A
135
Residue number B
150
Peptide name
Huntingtin
Ligandability
Cysteine 135 of Huntingtin
Cysteine 150 of Huntingtin
6x9o A 109 A 137
A redox-regulated disulphide may form within Huntingtin between cysteines 107 and 135 (109 and 137 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
6x9o
Structure name
high resolution cryoem structure of huntingtin in complex with hap40
Structure deposition date
2020-06-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P42858
Residue number A
107
Residue number B
135
Peptide name
Huntingtin
Ligandability
Cysteine 107 of Huntingtin
Cysteine 135 of Huntingtin
7dxj A 819 A 823
A redox-regulated disulphide may form within Huntingtin between cysteines 823 and 827 (819 and 823 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
7dxj
Structure name
human 46qhuntingtin-hap40 complex structure
Structure deposition date
2021-01-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
87
Minimum pKa ?
10
% buried
72
Peptide accession
P42858
Residue number A
823
Residue number B
827
Peptide name
Huntingtin
Ligandability
Cysteine 823 of Huntingtin
Cysteine 827 of Huntingtin
7dxj A 2277 A 2278
A redox-regulated disulphide may form within Huntingtin between cysteines 2281 and 2282 (2277 and 2278 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
7dxj
Structure name
human 46qhuntingtin-hap40 complex structure
Structure deposition date
2021-01-19
Thiol separation (Å)
7
Half-sphere exposure sum ?
94
Minimum pKa ?
12
% buried
100
Peptide accession
P42858
Residue number A
2281
Residue number B
2282
Peptide name
Huntingtin
Ligandability
Cysteine 2281 of Huntingtin
Cysteine 2282 of Huntingtin
6rmh A 2278 A 2279
A redox-regulated disulphide may form within Huntingtin between cysteines 2282 and 2283 (2278 and 2279 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
6rmh
Structure name
the rigid-body refined model of the normal huntingtin
Structure deposition date
2019-05-06
Thiol separation (Å)
8
Half-sphere exposure sum ?
89
Minimum pKa ?
12
% buried
100
Peptide accession
P42858
Residue number A
2282
Residue number B
2283
Peptide name
Huntingtin
Ligandability
Cysteine 2282 of Huntingtin
Cysteine 2283 of Huntingtin
7dxj A 2829 A 2873
A redox-regulated disulphide may form within Huntingtin between cysteines 2833 and 2877 (2829 and 2873 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
36
PDB code
7dxj
Structure name
human 46qhuntingtin-hap40 complex structure
Structure deposition date
2021-01-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
84
Minimum pKa ?
8
% buried
100
Peptide accession
P42858
Residue number A
2833
Residue number B
2877
Peptide name
Huntingtin
Ligandability
Cysteine 2833 of Huntingtin
Cysteine 2877 of Huntingtin
7dxj A 2301 A 2356
A redox-regulated disulphide may form within Huntingtin between cysteines 2305 and 2360 (2301 and 2356 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
7dxj
Structure name
human 46qhuntingtin-hap40 complex structure
Structure deposition date
2021-01-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
78
Minimum pKa ?
12
% buried
80
Peptide accession
P42858
Residue number A
2305
Residue number B
2360
Peptide name
Huntingtin
Ligandability
Cysteine 2305 of Huntingtin
Cysteine 2360 of Huntingtin
6x9o A 2861 A 2879
A redox-regulated disulphide may form within Huntingtin between cysteines 2859 and 2877 (2861 and 2879 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
31
PDB code
6x9o
Structure name
high resolution cryoem structure of huntingtin in complex with hap40
Structure deposition date
2020-06-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
80
Minimum pKa ?
13
% buried
100
Peptide accession
P42858
Residue number A
2859
Residue number B
2877
Peptide name
Huntingtin
Ligandability
Cysteine 2859 of Huntingtin
Cysteine 2877 of Huntingtin
7dxk A 829 A 834
A redox-regulated disulphide may form within Huntingtin between cysteines 833 and 838 (829 and 834 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
30
PDB code
7dxk
Structure name
human 128qhuntingtin-hap40 complex structure
Structure deposition date
2021-01-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
80
Minimum pKa ?
12
% buried
100
Peptide accession
P42858
Residue number A
833
Residue number B
838
Peptide name
Huntingtin
Ligandability
Cysteine 833 of Huntingtin
Cysteine 838 of Huntingtin
7dxk A 1022 A 1026
A redox-regulated disulphide may form within Huntingtin between cysteines 1026 and 1030 (1022 and 1026 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
30
PDB code
7dxk
Structure name
human 128qhuntingtin-hap40 complex structure
Structure deposition date
2021-01-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
79
Minimum pKa ?
13
% buried
96
Peptide accession
P42858
Residue number A
1026
Residue number B
1030
Peptide name
Huntingtin
Ligandability
Cysteine 1026 of Huntingtin
Cysteine 1030 of Huntingtin
7dxj A 1296 A 1307
A redox-regulated disulphide may form within Huntingtin between cysteines 1300 and 1311 (1296 and 1307 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
30
PDB code
7dxj
Structure name
human 46qhuntingtin-hap40 complex structure
Structure deposition date
2021-01-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
77
Minimum pKa ?
12
% buried
96
Peptide accession
P42858
Residue number A
1300
Residue number B
1311
Peptide name
Huntingtin
Ligandability
Cysteine 1300 of Huntingtin
Cysteine 1311 of Huntingtin
6x9o A 2284 A 2312
A redox-regulated disulphide may form within Huntingtin between cysteines 2282 and 2310 (2284 and 2312 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
28
PDB code
6x9o
Structure name
high resolution cryoem structure of huntingtin in complex with hap40
Structure deposition date
2020-06-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
96
Minimum pKa ?
13
% buried
100
Peptide accession
P42858
Residue number A
2282
Residue number B
2310
Peptide name
Huntingtin
Ligandability
Cysteine 2282 of Huntingtin
Cysteine 2310 of Huntingtin
7dxk A 2277 A 2279
A redox-regulated disulphide may form within Huntingtin between cysteines 2281 and 2283 (2277 and 2279 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
23
PDB code
7dxk
Structure name
human 128qhuntingtin-hap40 complex structure
Structure deposition date
2021-01-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
88
Minimum pKa ?
12
% buried
100
Peptide accession
P42858
Residue number A
2281
Residue number B
2283
Peptide name
Huntingtin
Ligandability
Cysteine 2281 of Huntingtin
Cysteine 2283 of Huntingtin
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