Potassium voltage-gated channel subfamily H member 2
Intramolecular
Cysteine 44 and cysteine 49
Cysteine 39 and cysteine 64
Cysteine 64 and cysteine 105
Cysteine 49 and cysteine 52
Cysteine 52 and cysteine 66
Cysteine 44 and cysteine 52
Cysteine 64 and cysteine 66
Cysteine 44 and cysteine 64
Cysteine 44 and cysteine 66
Cysteine 105 and cysteine 108
More...Cysteine 52 and cysteine 108
Cysteine 52 and cysteine 105
Cysteine 39 and cysteine 66
Cysteine 66 and cysteine 108
Cysteine 49 and cysteine 66
4hqa A 44 A 49
A redox-regulated disulphide may form within Potassium voltage-gated channel subfamily H member 2 between cysteines 44 and 49.
Details
Redox score ?
77
PDB code
4hqa
Structure name
crystal structure of pas domain from the human erg (herg) potassium channel
Structure deposition date
2012-10-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
10
% buried
28
Peptide accession
Q12809
Residue number A
44
Residue number B
49
Peptide name
Potassium voltage-gated channel subfamily H member 2
Ligandability
Cysteine 44 of Potassium voltage-gated channel subfamily H member 2
Cysteine 49 of Potassium voltage-gated channel subfamily H member 2
1byw A 39 A 64
A redox-regulated disulphide may form within Potassium voltage-gated channel subfamily H member 2 between cysteines 39 and 64.
Details
Redox score ?
70
PDB code
1byw
Structure name
structure of the n-terminal domain of the human-erg potassium channel
Structure deposition date
1998-10-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
73
Minimum pKa ?
10
% buried
52
Peptide accession
Q12809
Residue number A
39
Residue number B
64
Peptide name
Potassium voltage-gated channel subfamily H member 2
Ligandability
Cysteine 39 of Potassium voltage-gated channel subfamily H member 2
Cysteine 64 of Potassium voltage-gated channel subfamily H member 2
1byw A 73 A 105
A redox-regulated disulphide may form within Potassium voltage-gated channel subfamily H member 2 between cysteines 64 and 105 (73 and 105 respectively in this structure).
Details
Redox score ?
69
PDB code
1byw
Structure name
structure of the n-terminal domain of the human-erg potassium channel
Structure deposition date
1998-10-15
Thiol separation (Å)
5
Half-sphere exposure sum ?
48
Minimum pKa ?
9
% buried
2
Peptide accession
Q12809
Residue number A
64
Residue number B
105
Peptide name
Potassium voltage-gated channel subfamily H member 2
Ligandability
Cysteine 64 of Potassium voltage-gated channel subfamily H member 2
Cysteine 105 of Potassium voltage-gated channel subfamily H member 2
4hp9 A 49 A 52
A redox-regulated disulphide may form within Potassium voltage-gated channel subfamily H member 2 between cysteines 49 and 52.
Details
Redox score ?
62
PDB code
4hp9
Structure name
crystal structure of the n-terminal truncated pas domain from the herg potassium channel
Structure deposition date
2012-10-23
Thiol separation (Å)
6
Half-sphere exposure sum ?
63
Minimum pKa ?
10
% buried
44
Peptide accession
Q12809
Residue number A
49
Residue number B
52
Peptide name
Potassium voltage-gated channel subfamily H member 2
Ligandability
Cysteine 49 of Potassium voltage-gated channel subfamily H member 2
Cysteine 52 of Potassium voltage-gated channel subfamily H member 2
1byw A 52 A 66
A redox-regulated disulphide may form within Potassium voltage-gated channel subfamily H member 2 between cysteines 52 and 66. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
1byw
Structure name
structure of the n-terminal domain of the human-erg potassium channel
Structure deposition date
1998-10-15
Thiol separation (Å)
7
Half-sphere exposure sum ?
75
Minimum pKa ?
11
% buried
79
Peptide accession
Q12809
Residue number A
52
Residue number B
66
Peptide name
Potassium voltage-gated channel subfamily H member 2
Ligandability
Cysteine 52 of Potassium voltage-gated channel subfamily H member 2
Cysteine 66 of Potassium voltage-gated channel subfamily H member 2
4hp9 A 44 A 52
A redox-regulated disulphide may form within Potassium voltage-gated channel subfamily H member 2 between cysteines 44 and 52. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
4hp9
Structure name
crystal structure of the n-terminal truncated pas domain from the herg potassium channel
Structure deposition date
2012-10-23
Thiol separation (Å)
8
Half-sphere exposure sum ?
76
Minimum pKa ?
11
% buried
52
Peptide accession
Q12809
Residue number A
44
Residue number B
52
Peptide name
Potassium voltage-gated channel subfamily H member 2
Ligandability
Cysteine 44 of Potassium voltage-gated channel subfamily H member 2
Cysteine 52 of Potassium voltage-gated channel subfamily H member 2
4hqa A 64 A 66
A redox-regulated disulphide may form within Potassium voltage-gated channel subfamily H member 2 between cysteines 64 and 66. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
4hqa
Structure name
crystal structure of pas domain from the human erg (herg) potassium channel
Structure deposition date
2012-10-25
Thiol separation (Å)
7
Half-sphere exposure sum ?
79
Minimum pKa ?
12
% buried
90
Peptide accession
Q12809
Residue number A
64
Residue number B
66
Peptide name
Potassium voltage-gated channel subfamily H member 2
Ligandability
Cysteine 64 of Potassium voltage-gated channel subfamily H member 2
Cysteine 66 of Potassium voltage-gated channel subfamily H member 2
2l0w A 44 A 64
A redox-regulated disulphide may form within Potassium voltage-gated channel subfamily H member 2 between cysteines 44 and 64. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
2l0w
Structure name
solution nmr structure of the n-terminal pas domain of herg potassium channel
Structure deposition date
2010-07-19
Thiol separation (Å)
8
Half-sphere exposure sum ?
73
Minimum pKa ?
10
% buried
60
Peptide accession
D3DX04
Residue number A
44
Residue number B
64
Peptide name
Potassium voltage-gated channel subfamily H member 2
Ligandability
Cysteine 44 of Potassium voltage-gated channel subfamily H member 2
Cysteine 64 of Potassium voltage-gated channel subfamily H member 2
1byw A 44 A 66
A redox-regulated disulphide may form within Potassium voltage-gated channel subfamily H member 2 between cysteines 44 and 66. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
1byw
Structure name
structure of the n-terminal domain of the human-erg potassium channel
Structure deposition date
1998-10-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
11
% buried
64
Peptide accession
Q12809
Residue number A
44
Residue number B
66
Peptide name
Potassium voltage-gated channel subfamily H member 2
Ligandability
Cysteine 44 of Potassium voltage-gated channel subfamily H member 2
Cysteine 66 of Potassium voltage-gated channel subfamily H member 2
4hp9 A 105 A 108
A redox-regulated disulphide may form within Potassium voltage-gated channel subfamily H member 2 between cysteines 105 and 108. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
4hp9
Structure name
crystal structure of the n-terminal truncated pas domain from the herg potassium channel
Structure deposition date
2012-10-23
Thiol separation (Å)
10
Half-sphere exposure sum ?
57
Minimum pKa ?
9
% buried
41
Peptide accession
Q12809
Residue number A
105
Residue number B
108
Peptide name
Potassium voltage-gated channel subfamily H member 2
Ligandability
Cysteine 105 of Potassium voltage-gated channel subfamily H member 2
Cysteine 108 of Potassium voltage-gated channel subfamily H member 2
2l0w A 52 A 108
A redox-regulated disulphide may form within Potassium voltage-gated channel subfamily H member 2 between cysteines 52 and 108. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
2l0w
Structure name
solution nmr structure of the n-terminal pas domain of herg potassium channel
Structure deposition date
2010-07-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
68
Minimum pKa ?
11
% buried
74
Peptide accession
D3DX04
Residue number A
52
Residue number B
108
Peptide name
Potassium voltage-gated channel subfamily H member 2
Ligandability
Cysteine 52 of Potassium voltage-gated channel subfamily H member 2
Cysteine 108 of Potassium voltage-gated channel subfamily H member 2
2l4r A 52 A 105
A redox-regulated disulphide may form within Potassium voltage-gated channel subfamily H member 2 between cysteines 52 and 105. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
2l4r
Structure name
nmr solution structure of the n-terminal pas domain of herg
Structure deposition date
2010-10-13
Thiol separation (Å)
10
Half-sphere exposure sum ?
52
Minimum pKa ?
10
% buried
31
Peptide accession
Q12809
Residue number A
52
Residue number B
105
Peptide name
Potassium voltage-gated channel subfamily H member 2
Ligandability
Cysteine 52 of Potassium voltage-gated channel subfamily H member 2
Cysteine 105 of Potassium voltage-gated channel subfamily H member 2
2l1m A 39 A 66
A redox-regulated disulphide may form within Potassium voltage-gated channel subfamily H member 2 between cysteines 39 and 66. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
2l1m
Structure name
solution structure of the eag domain of the herg (kv11
Structure deposition date
2010-07-29
Thiol separation (Å)
10
Half-sphere exposure sum ?
72
Minimum pKa ?
10
% buried
62
Peptide accession
Q12809
Residue number A
39
Residue number B
66
Peptide name
Potassium voltage-gated channel subfamily H member 2
Ligandability
Cysteine 39 of Potassium voltage-gated channel subfamily H member 2
Cysteine 66 of Potassium voltage-gated channel subfamily H member 2
2l0w A 66 A 108
A redox-regulated disulphide may form within Potassium voltage-gated channel subfamily H member 2 between cysteines 66 and 108. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
36
PDB code
2l0w
Structure name
solution nmr structure of the n-terminal pas domain of herg potassium channel
Structure deposition date
2010-07-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
70
Minimum pKa ?
12
% buried
87
Peptide accession
D3DX04
Residue number A
66
Residue number B
108
Peptide name
Potassium voltage-gated channel subfamily H member 2
Ligandability
Cysteine 66 of Potassium voltage-gated channel subfamily H member 2
Cysteine 108 of Potassium voltage-gated channel subfamily H member 2
4hqa A 49 A 66
A redox-regulated disulphide may form within Potassium voltage-gated channel subfamily H member 2 between cysteines 49 and 66. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
35
PDB code
4hqa
Structure name
crystal structure of pas domain from the human erg (herg) potassium channel
Structure deposition date
2012-10-25
Thiol separation (Å)
10
Half-sphere exposure sum ?
65
Minimum pKa ?
11
% buried
62
Peptide accession
Q12809
Residue number A
49
Residue number B
66
Peptide name
Potassium voltage-gated channel subfamily H member 2
Ligandability
Cysteine 49 of Potassium voltage-gated channel subfamily H member 2
Cysteine 66 of Potassium voltage-gated channel subfamily H member 2
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