Obscurin
Intramolecular
Cysteine 3295 and cysteine 3415
Cysteine 3735 and cysteine 3767
Cysteine 3471 and cysteine 3520
Cysteine 3647 and cysteine 3696
Cysteine 2937 and cysteine 2987
Cysteine 3647 and cysteine 3679
Cysteine 3823 and cysteine 3855
Cysteine 3295 and cysteine 3432
Cysteine 3559 and cysteine 3591
Cysteine 3735 and cysteine 3784
More...Cysteine 3295 and cysteine 3855
Cysteine 31 and cysteine 82
Cysteine 3295 and cysteine 3784
Cysteine 1096 and cysteine 962
Cysteine 3471 and cysteine 3503
Cysteine 3559 and cysteine 3608
Cysteine 3767 and cysteine 3784
Cysteine 3415 and cysteine 3432
Cysteine 2848 and cysteine 2898
Cysteine 3823 and cysteine 3608
Cysteine 3855 and cysteine 3608
Cysteine 3855 and cysteine 3610
Cysteine 3767 and cysteine 3610
Cysteine 3206 and cysteine 3256
Cysteine 3503 and cysteine 3522
Cysteine 3679 and cysteine 3696
Cysteine 3679 and cysteine 3698
Cysteine 3591 and cysteine 3608
Cysteine 3784 and cysteine 3610
Cysteine 3855 and cysteine 3784
Cysteine 3471 and cysteine 3522
Cysteine 3520 and cysteine 3522
Cysteine 3503 and cysteine 3520
Cysteine 3218 and cysteine 3256
Cysteine 3591 and cysteine 3610
Cysteine 3696 and cysteine 3698
Cysteine 3295 and cysteine 3610
Cysteine 3559 and cysteine 3610
Cysteine 3647 and cysteine 3698
Cysteine 1188 and cysteine 1127
2edr A 30 A 62
A redox-regulated disulphide may form within Obscurin between cysteines 3295 and 3415 (30 and 62 respectively in this structure).
Details
Redox score ?
75
PDB code
2edr
Structure name
solution structure of the ig-like domain (3361-3449) of human obscurin
Structure deposition date
2007-02-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
75
Minimum pKa ?
8
% buried
48
Peptide accession
Q5VST9
Residue number A
3295
Residue number B
3415
Peptide name
Obscurin
Ligandability
Cysteine 3295 of Obscurin
Cysteine 3415 of Obscurin
2edq A 30 A 62
A redox-regulated disulphide may form within Obscurin between cysteines 3735 and 3767 (30 and 62 respectively in this structure).
Details
Redox score ?
75
PDB code
2edq
Structure name
solution structure of the ig-like domain (3713-3806) of human obscurin
Structure deposition date
2007-02-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
72
Minimum pKa ?
10
% buried
47
Peptide accession
Q5VST9
Residue number A
3735
Residue number B
3767
Peptide name
Obscurin
Ligandability
Cysteine 3735 of Obscurin
Cysteine 3767 of Obscurin
2edt A 30 A 79
A redox-regulated disulphide may form within Obscurin between cysteines 3471 and 3520 (30 and 79 respectively in this structure).
Details
Redox score ?
74
PDB code
2edt
Structure name
solution structure of the ig-like domain (3449-3537) from human obscurin
Structure deposition date
2007-02-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
79
Minimum pKa ?
8
% buried
65
Peptide accession
Q5VST9
Residue number A
3471
Residue number B
3520
Peptide name
Obscurin
Ligandability
Cysteine 3471 of Obscurin
Cysteine 3520 of Obscurin
2edh A 41 A 90
A redox-regulated disulphide may form within Obscurin between cysteines 3647 and 3696 (41 and 90 respectively in this structure).
Details
Redox score ?
74
PDB code
2edh
Structure name
solution structure of the pdz domain (3614- 3713 ) from human obscurin
Structure deposition date
2007-02-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
74
Minimum pKa ?
7
% buried
58
Peptide accession
Q5VST9
Residue number A
3647
Residue number B
3696
Peptide name
Obscurin
Ligandability
Cysteine 3647 of Obscurin
Cysteine 3696 of Obscurin
2dku A 30 A 80
A redox-regulated disulphide may form within Obscurin between cysteines 2937 and 2987 (30 and 80 respectively in this structure).
Details
Redox score ?
74
PDB code
2dku
Structure name
solution structure of the third ig-like domain of human kiaa1556 protein
Structure deposition date
2006-04-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
80
Minimum pKa ?
8
% buried
64
Peptide accession
Q5VST9
Residue number A
2937
Residue number B
2987
Peptide name
Obscurin
Ligandability
Cysteine 2937 of Obscurin
Cysteine 2987 of Obscurin
2edh A 41 A 73
A redox-regulated disulphide may form within Obscurin between cysteines 3647 and 3679 (41 and 73 respectively in this structure).
Details
Redox score ?
73
PDB code
2edh
Structure name
solution structure of the pdz domain (3614- 3713 ) from human obscurin
Structure deposition date
2007-02-14
Thiol separation (Å)
5
Half-sphere exposure sum ?
69
Minimum pKa ?
7
% buried
45
Peptide accession
Q5VST9
Residue number A
3647
Residue number B
3679
Peptide name
Obscurin
Ligandability
Cysteine 3647 of Obscurin
Cysteine 3679 of Obscurin
2edl A 30 A 62
A redox-regulated disulphide may form within Obscurin between cysteines 3823 and 3855 (30 and 62 respectively in this structure).
Details
Redox score ?
72
PDB code
2edl
Structure name
solution structure of the ig-like domain (3801-3897) of human obscurin
Structure deposition date
2007-02-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
11
% buried
47
Peptide accession
Q5VST9
Residue number A
3823
Residue number B
3855
Peptide name
Obscurin
Ligandability
Cysteine 3823 of Obscurin
Cysteine 3855 of Obscurin
2edr A 30 A 79
A redox-regulated disulphide may form within Obscurin between cysteines 3295 and 3432 (30 and 79 respectively in this structure).
Details
Redox score ?
72
PDB code
2edr
Structure name
solution structure of the ig-like domain (3361-3449) of human obscurin
Structure deposition date
2007-02-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
84
Minimum pKa ?
8
% buried
62
Peptide accession
Q5VST9
Residue number A
3295
Residue number B
3432
Peptide name
Obscurin
Ligandability
Cysteine 3295 of Obscurin
Cysteine 3432 of Obscurin
2edw A 30 A 62
A redox-regulated disulphide may form within Obscurin between cysteines 3559 and 3591 (30 and 62 respectively in this structure).
Details
Redox score ?
71
PDB code
2edw
Structure name
solution structure of the i-set domain (3537-3630) of human obscurin
Structure deposition date
2007-02-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
72
Minimum pKa ?
10
% buried
46
Peptide accession
Q5VST9
Residue number A
3559
Residue number B
3591
Peptide name
Obscurin
Ligandability
Cysteine 3559 of Obscurin
Cysteine 3591 of Obscurin
2edq A 30 A 79
A redox-regulated disulphide may form within Obscurin between cysteines 3735 and 3784 (30 and 79 respectively in this structure).
Details
Redox score ?
70
PDB code
2edq
Structure name
solution structure of the ig-like domain (3713-3806) of human obscurin
Structure deposition date
2007-02-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
78
Minimum pKa ?
10
% buried
60
Peptide accession
Q5VST9
Residue number A
3735
Residue number B
3784
Peptide name
Obscurin
Ligandability
Cysteine 3735 of Obscurin
Cysteine 3784 of Obscurin
2dm7 A 30 A 62
A redox-regulated disulphide may form within Obscurin between cysteines 3295 and 3855 (30 and 62 respectively in this structure).
Details
Redox score ?
69
PDB code
2dm7
Structure name
solution structure of the 14th ig-like domain of human kiaa1556 protein
Structure deposition date
2006-04-20
Thiol separation (Å)
5
Half-sphere exposure sum ?
70
Minimum pKa ?
9
% buried
48
Peptide accession
Q8NHN3
Residue number A
3295
Residue number B
3855
Peptide name
Obscurin
Ligandability
Cysteine 3295 of Obscurin
Cysteine 3855 of Obscurin
4c4k O 31 O 82
A redox-regulated disulphide may form within Obscurin between cysteines 31 and 82.
Details
Redox score ?
68
PDB code
4c4k
Structure name
crystal structure of the titin m10-obscurin ig domain 1 complex
Structure deposition date
2013-09-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
87
Minimum pKa ?
9
% buried
94
Peptide accession
Q5VST9
Residue number A
31
Residue number B
82
Peptide name
Obscurin
Ligandability
Cysteine 31 of Obscurin
Cysteine 82 of Obscurin
2dm7 A 30 A 79
A redox-regulated disulphide may form within Obscurin between cysteines 3295 and 3784 (30 and 79 respectively in this structure).
Details
Redox score ?
68
PDB code
2dm7
Structure name
solution structure of the 14th ig-like domain of human kiaa1556 protein
Structure deposition date
2006-04-20
Thiol separation (Å)
5
Half-sphere exposure sum ?
78
Minimum pKa ?
9
% buried
60
Peptide accession
Q8NHN3
Residue number A
3295
Residue number B
3784
Peptide name
Obscurin
Ligandability
Cysteine 3295 of Obscurin
Cysteine 3784 of Obscurin
7r68 A 27 A 77
A redox-regulated disulphide may form within Obscurin between cysteines 1096 and 962 (27 and 77 respectively in this structure).
Details
Redox score ?
67
PDB code
7r68
Structure name
human obscurin ig12
Structure deposition date
2021-06-22
Thiol separation (Å)
5
Half-sphere exposure sum ?
70
Minimum pKa ?
10
% buried
46
Peptide accession
Q5VST9
Residue number A
1096
Residue number B
962
Peptide name
Obscurin
Ligandability
Cysteine 1096 of Obscurin
Cysteine 962 of Obscurin
2edt A 30 A 62
A redox-regulated disulphide may form within Obscurin between cysteines 3471 and 3503 (30 and 62 respectively in this structure).
Details
Redox score ?
67
PDB code
2edt
Structure name
solution structure of the ig-like domain (3449-3537) from human obscurin
Structure deposition date
2007-02-15
Thiol separation (Å)
5
Half-sphere exposure sum ?
75
Minimum pKa ?
8
% buried
50
Peptide accession
Q5VST9
Residue number A
3471
Residue number B
3503
Peptide name
Obscurin
Ligandability
Cysteine 3471 of Obscurin
Cysteine 3503 of Obscurin
2edw A 30 A 79
A redox-regulated disulphide may form within Obscurin between cysteines 3559 and 3608 (30 and 79 respectively in this structure).
Details
Redox score ?
65
PDB code
2edw
Structure name
solution structure of the i-set domain (3537-3630) of human obscurin
Structure deposition date
2007-02-15
Thiol separation (Å)
5
Half-sphere exposure sum ?
80
Minimum pKa ?
10
% buried
59
Peptide accession
Q5VST9
Residue number A
3559
Residue number B
3608
Peptide name
Obscurin
Ligandability
Cysteine 3559 of Obscurin
Cysteine 3608 of Obscurin
2edq A 62 A 79
A redox-regulated disulphide may form within Obscurin between cysteines 3767 and 3784 (62 and 79 respectively in this structure).
Details
Redox score ?
65
PDB code
2edq
Structure name
solution structure of the ig-like domain (3713-3806) of human obscurin
Structure deposition date
2007-02-14
Thiol separation (Å)
5
Half-sphere exposure sum ?
72
Minimum pKa ?
10
% buried
54
Peptide accession
Q5VST9
Residue number A
3767
Residue number B
3784
Peptide name
Obscurin
Ligandability
Cysteine 3767 of Obscurin
Cysteine 3784 of Obscurin
2edr A 62 A 79
A redox-regulated disulphide may form within Obscurin between cysteines 3415 and 3432 (62 and 79 respectively in this structure).
Details
Redox score ?
65
PDB code
2edr
Structure name
solution structure of the ig-like domain (3361-3449) of human obscurin
Structure deposition date
2007-02-14
Thiol separation (Å)
5
Half-sphere exposure sum ?
77
Minimum pKa ?
10
% buried
56
Peptide accession
Q5VST9
Residue number A
3415
Residue number B
3432
Peptide name
Obscurin
Ligandability
Cysteine 3415 of Obscurin
Cysteine 3432 of Obscurin
2edf A 30 A 80
A redox-regulated disulphide may form within Obscurin between cysteines 2848 and 2898 (30 and 80 respectively in this structure).
Details
Redox score ?
65
PDB code
2edf
Structure name
solution structure of the second ig-like domain(2826-2915) from human obscurin
Structure deposition date
2007-02-14
Thiol separation (Å)
5
Half-sphere exposure sum ?
76
Minimum pKa ?
9
% buried
56
Peptide accession
Q5VST9
Residue number A
2848
Residue number B
2898
Peptide name
Obscurin
Ligandability
Cysteine 2848 of Obscurin
Cysteine 2898 of Obscurin
2edl A 30 A 79
A redox-regulated disulphide may form within Obscurin between cysteines 3823 and 3608 (30 and 79 respectively in this structure).
Details
Redox score ?
61
PDB code
2edl
Structure name
solution structure of the ig-like domain (3801-3897) of human obscurin
Structure deposition date
2007-02-14
Thiol separation (Å)
5
Half-sphere exposure sum ?
74
Minimum pKa ?
11
% buried
61
Peptide accession
Q5VST9
Residue number A
3823
Residue number B
3608
Peptide name
Obscurin
Ligandability
Cysteine 3823 of Obscurin
Cysteine 3608 of Obscurin
2edl A 62 A 79
A redox-regulated disulphide may form within Obscurin between cysteines 3855 and 3608 (62 and 79 respectively in this structure).
Details
Redox score ?
61
PDB code
2edl
Structure name
solution structure of the ig-like domain (3801-3897) of human obscurin
Structure deposition date
2007-02-14
Thiol separation (Å)
5
Half-sphere exposure sum ?
73
Minimum pKa ?
11
% buried
54
Peptide accession
Q5VST9
Residue number A
3855
Residue number B
3608
Peptide name
Obscurin
Ligandability
Cysteine 3855 of Obscurin
Cysteine 3608 of Obscurin
2edl A 62 A 81
A redox-regulated disulphide may form within Obscurin between cysteines 3855 and 3610 (62 and 81 respectively in this structure).
Details
Redox score ?
60
PDB code
2edl
Structure name
solution structure of the ig-like domain (3801-3897) of human obscurin
Structure deposition date
2007-02-14
Thiol separation (Å)
6
Half-sphere exposure sum ?
64
Minimum pKa ?
11
% buried
29
Peptide accession
Q5VST9
Residue number A
3855
Residue number B
3610
Peptide name
Obscurin
Ligandability
Cysteine 3855 of Obscurin
Cysteine 3610 of Obscurin
2edq A 62 A 81
A redox-regulated disulphide may form within Obscurin between cysteines 3767 and 3610 (62 and 81 respectively in this structure).
Details
Redox score ?
60
PDB code
2edq
Structure name
solution structure of the ig-like domain (3713-3806) of human obscurin
Structure deposition date
2007-02-14
Thiol separation (Å)
7
Half-sphere exposure sum ?
62
Minimum pKa ?
9
% buried
28
Peptide accession
Q5VST9
Residue number A
3767
Residue number B
3610
Peptide name
Obscurin
Ligandability
Cysteine 3767 of Obscurin
Cysteine 3610 of Obscurin
2e7b A 30 A 80
A redox-regulated disulphide may form within Obscurin between cysteines 3206 and 3256 (30 and 80 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
60
PDB code
2e7b
Structure name
solution structure of the 6th ig-like domain from human kiaa1556
Structure deposition date
2007-01-09
Thiol separation (Å)
6
Half-sphere exposure sum ?
70
Minimum pKa ?
11
% buried
55
Peptide accession
Q8NHN3
Residue number A
3206
Residue number B
3256
Peptide name
Obscurin
Ligandability
Cysteine 3206 of Obscurin
Cysteine 3256 of Obscurin
2edt A 62 A 81
A redox-regulated disulphide may form within Obscurin between cysteines 3503 and 3522 (62 and 81 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
59
PDB code
2edt
Structure name
solution structure of the ig-like domain (3449-3537) from human obscurin
Structure deposition date
2007-02-15
Thiol separation (Å)
6
Half-sphere exposure sum ?
66
Minimum pKa ?
10
% buried
30
Peptide accession
Q5VST9
Residue number A
3503
Residue number B
3522
Peptide name
Obscurin
Ligandability
Cysteine 3503 of Obscurin
Cysteine 3522 of Obscurin
2edh A 73 A 90
A redox-regulated disulphide may form within Obscurin between cysteines 3679 and 3696 (73 and 90 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
59
PDB code
2edh
Structure name
solution structure of the pdz domain (3614- 3713 ) from human obscurin
Structure deposition date
2007-02-14
Thiol separation (Å)
6
Half-sphere exposure sum ?
69
Minimum pKa ?
11
% buried
50
Peptide accession
Q5VST9
Residue number A
3679
Residue number B
3696
Peptide name
Obscurin
Ligandability
Cysteine 3679 of Obscurin
Cysteine 3696 of Obscurin
2edh A 73 A 92
A redox-regulated disulphide may form within Obscurin between cysteines 3679 and 3698 (73 and 92 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
58
PDB code
2edh
Structure name
solution structure of the pdz domain (3614- 3713 ) from human obscurin
Structure deposition date
2007-02-14
Thiol separation (Å)
7
Half-sphere exposure sum ?
62
Minimum pKa ?
10
% buried
27
Peptide accession
Q5VST9
Residue number A
3679
Residue number B
3698
Peptide name
Obscurin
Ligandability
Cysteine 3679 of Obscurin
Cysteine 3698 of Obscurin
2edw A 62 A 79
A redox-regulated disulphide may form within Obscurin between cysteines 3591 and 3608 (62 and 79 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
57
PDB code
2edw
Structure name
solution structure of the i-set domain (3537-3630) of human obscurin
Structure deposition date
2007-02-15
Thiol separation (Å)
5
Half-sphere exposure sum ?
76
Minimum pKa ?
13
% buried
56
Peptide accession
Q5VST9
Residue number A
3591
Residue number B
3608
Peptide name
Obscurin
Ligandability
Cysteine 3591 of Obscurin
Cysteine 3608 of Obscurin
2edq A 79 A 81
A redox-regulated disulphide may form within Obscurin between cysteines 3784 and 3610 (79 and 81 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
56
PDB code
2edq
Structure name
solution structure of the ig-like domain (3713-3806) of human obscurin
Structure deposition date
2007-02-14
Thiol separation (Å)
7
Half-sphere exposure sum ?
68
Minimum pKa ?
9
% buried
40
Peptide accession
Q5VST9
Residue number A
3784
Residue number B
3610
Peptide name
Obscurin
Ligandability
Cysteine 3784 of Obscurin
Cysteine 3610 of Obscurin
2dm7 A 62 A 79
A redox-regulated disulphide may form within Obscurin between cysteines 3855 and 3784 (62 and 79 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
56
PDB code
2dm7
Structure name
solution structure of the 14th ig-like domain of human kiaa1556 protein
Structure deposition date
2006-04-20
Thiol separation (Å)
6
Half-sphere exposure sum ?
74
Minimum pKa ?
12
% buried
54
Peptide accession
Q8NHN3
Residue number A
3855
Residue number B
3784
Peptide name
Obscurin
Ligandability
Cysteine 3855 of Obscurin
Cysteine 3784 of Obscurin
2edt A 30 A 81
A redox-regulated disulphide may form within Obscurin between cysteines 3471 and 3522 (30 and 81 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
56
PDB code
2edt
Structure name
solution structure of the ig-like domain (3449-3537) from human obscurin
Structure deposition date
2007-02-15
Thiol separation (Å)
7
Half-sphere exposure sum ?
73
Minimum pKa ?
8
% buried
40
Peptide accession
Q5VST9
Residue number A
3471
Residue number B
3522
Peptide name
Obscurin
Ligandability
Cysteine 3471 of Obscurin
Cysteine 3522 of Obscurin
2edt A 79 A 81
A redox-regulated disulphide may form within Obscurin between cysteines 3520 and 3522 (79 and 81 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
56
PDB code
2edt
Structure name
solution structure of the ig-like domain (3449-3537) from human obscurin
Structure deposition date
2007-02-15
Thiol separation (Å)
7
Half-sphere exposure sum ?
70
Minimum pKa ?
10
% buried
46
Peptide accession
Q5VST9
Residue number A
3520
Residue number B
3522
Peptide name
Obscurin
Ligandability
Cysteine 3520 of Obscurin
Cysteine 3522 of Obscurin
2edt A 62 A 79
A redox-regulated disulphide may form within Obscurin between cysteines 3503 and 3520 (62 and 79 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
2edt
Structure name
solution structure of the ig-like domain (3449-3537) from human obscurin
Structure deposition date
2007-02-15
Thiol separation (Å)
6
Half-sphere exposure sum ?
72
Minimum pKa ?
12
% buried
56
Peptide accession
Q5VST9
Residue number A
3503
Residue number B
3520
Peptide name
Obscurin
Ligandability
Cysteine 3503 of Obscurin
Cysteine 3520 of Obscurin
2e7b A 42 A 80
A redox-regulated disulphide may form within Obscurin between cysteines 3218 and 3256 (42 and 80 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
2e7b
Structure name
solution structure of the 6th ig-like domain from human kiaa1556
Structure deposition date
2007-01-09
Thiol separation (Å)
7
Half-sphere exposure sum ?
61
Minimum pKa ?
9
% buried
30
Peptide accession
Q8NHN3
Residue number A
3218
Residue number B
3256
Peptide name
Obscurin
Ligandability
Cysteine 3218 of Obscurin
Cysteine 3256 of Obscurin
2edw A 62 A 81
A redox-regulated disulphide may form within Obscurin between cysteines 3591 and 3610 (62 and 81 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
2edw
Structure name
solution structure of the i-set domain (3537-3630) of human obscurin
Structure deposition date
2007-02-15
Thiol separation (Å)
8
Half-sphere exposure sum ?
65
Minimum pKa ?
10
% buried
28
Peptide accession
Q5VST9
Residue number A
3591
Residue number B
3610
Peptide name
Obscurin
Ligandability
Cysteine 3591 of Obscurin
Cysteine 3610 of Obscurin
2edh A 90 A 92
A redox-regulated disulphide may form within Obscurin between cysteines 3696 and 3698 (90 and 92 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
2edh
Structure name
solution structure of the pdz domain (3614- 3713 ) from human obscurin
Structure deposition date
2007-02-14
Thiol separation (Å)
7
Half-sphere exposure sum ?
67
Minimum pKa ?
10
% buried
40
Peptide accession
Q5VST9
Residue number A
3696
Residue number B
3698
Peptide name
Obscurin
Ligandability
Cysteine 3696 of Obscurin
Cysteine 3698 of Obscurin
2dm7 A 30 A 81
A redox-regulated disulphide may form within Obscurin between cysteines 3295 and 3610 (30 and 81 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
53
PDB code
2dm7
Structure name
solution structure of the 14th ig-like domain of human kiaa1556 protein
Structure deposition date
2006-04-20
Thiol separation (Å)
8
Half-sphere exposure sum ?
68
Minimum pKa ?
9
% buried
35
Peptide accession
Q8NHN3
Residue number A
3295
Residue number B
3610
Peptide name
Obscurin
Ligandability
Cysteine 3295 of Obscurin
Cysteine 3610 of Obscurin
2edw A 30 A 81
A redox-regulated disulphide may form within Obscurin between cysteines 3559 and 3610 (30 and 81 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
53
PDB code
2edw
Structure name
solution structure of the i-set domain (3537-3630) of human obscurin
Structure deposition date
2007-02-15
Thiol separation (Å)
7
Half-sphere exposure sum ?
69
Minimum pKa ?
10
% buried
31
Peptide accession
Q5VST9
Residue number A
3559
Residue number B
3610
Peptide name
Obscurin
Ligandability
Cysteine 3559 of Obscurin
Cysteine 3610 of Obscurin
2edh A 41 A 92
A redox-regulated disulphide may form within Obscurin between cysteines 3647 and 3698 (41 and 92 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
52
PDB code
2edh
Structure name
solution structure of the pdz domain (3614- 3713 ) from human obscurin
Structure deposition date
2007-02-14
Thiol separation (Å)
9
Half-sphere exposure sum ?
67
Minimum pKa ?
7
% buried
34
Peptide accession
Q5VST9
Residue number A
3647
Residue number B
3698
Peptide name
Obscurin
Ligandability
Cysteine 3647 of Obscurin
Cysteine 3698 of Obscurin
7r67 A 29 A 60
A redox-regulated disulphide may form within Obscurin between cysteines 1188 and 1127 (29 and 60 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
52
PDB code
7r67
Structure name
human obscurin ig13
Structure deposition date
2021-06-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
56
Minimum pKa ?
9
% buried
20
Peptide accession
Q5VST9
Residue number A
1188
Residue number B
1127
Peptide name
Obscurin
Ligandability
Cysteine 1188 of Obscurin
Cysteine 1127 of Obscurin
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