ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Calcium-activated potassium channel subunit alpha-1

Intramolecular
Cysteine 680 and cysteine 695
Cysteine 118 and cysteine 119
Cysteine 677 and cysteine 695
Cysteine 413 and cysteine 487
Cysteine 845 and cysteine 923
Cysteine 693 and cysteine 695
Cysteine 920 and cysteine 923
Cysteine 680 and cysteine 693
Cysteine 677 and cysteine 693
Cysteine 1134 and cysteine 1174
More...
Cysteine 677 and cysteine 680
Cysteine 1034 and cysteine 1151
Cysteine 1118 and cysteine 1124
Cysteine 619 and cysteine 622
Cysteine 845 and cysteine 920
Cysteine 622 and cysteine 1124
Cysteine 845 and cysteine 943
Cysteine 619 and cysteine 1124
Cysteine 563 and cysteine 920
Cysteine 619 and cysteine 1098
Cysteine 1124 and cysteine 1134
Cysteine 1098 and cysteine 1174
Cysteine 563 and cysteine 923
Cysteine 619 and cysteine 1134
A redox-regulated disulphide may form within Calcium-activated potassium channel subunit alpha-1 between cysteines 680 and 695 (615 and 630 respectively in this structure).

Details

Redox score ?
79
PDB code
6v3g
Structure name
cryo-em structure of ca2+-free hsslo1 channel
Structure deposition date
2019-11-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
39
Minimum pKa ?
9
% buried
0
Peptide accession
Q12791
Residue number A
680
Residue number B
695
Peptide name
Calcium-activated potassium channel subunit alpha-1

Ligandability

Cysteine 680 of Calcium-activated potassium channel subunit alpha-1

Cysteine 695 of Calcium-activated potassium channel subunit alpha-1

A redox-regulated disulphide may form within Calcium-activated potassium channel subunit alpha-1 between cysteines 118 and 119 (53 and 54 respectively in this structure).

Details

Redox score ?
78
PDB code
6v22
Structure name
cryo-em structure of ca2+-bound hsslo1-beta4 channel complex
Structure deposition date
2019-11-22
Thiol separation (Å)
5
Half-sphere exposure sum ?
nan
Minimum pKa ?
9
% buried
0
Peptide accession
Q12791
Residue number A
118
Residue number B
119
Peptide name
Calcium-activated potassium channel subunit alpha-1

Ligandability

Cysteine 118 of Calcium-activated potassium channel subunit alpha-1

Cysteine 119 of Calcium-activated potassium channel subunit alpha-1

A redox-regulated disulphide may form within Calcium-activated potassium channel subunit alpha-1 between cysteines 677 and 695 (612 and 630 respectively in this structure).

Details

Redox score ?
70
PDB code
6v3g
Structure name
cryo-em structure of ca2+-free hsslo1 channel
Structure deposition date
2019-11-25
Thiol separation (Å)
6
Half-sphere exposure sum ?
45
Minimum pKa ?
8
% buried
0
Peptide accession
Q12791
Residue number A
677
Residue number B
695
Peptide name
Calcium-activated potassium channel subunit alpha-1

Ligandability

Cysteine 677 of Calcium-activated potassium channel subunit alpha-1

Cysteine 695 of Calcium-activated potassium channel subunit alpha-1

A redox-regulated disulphide may form within Calcium-activated potassium channel subunit alpha-1 between cysteines 413 and 487 (348 and 422 respectively in this structure).

Details

Redox score ?
70
PDB code
3naf
Structure name
structure of the intracellular gating ring from the human high- conductance ca2+ gated k+ channel (bk channel)
Structure deposition date
2010-06-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
94
Minimum pKa ?
8
% buried
100
Peptide accession
Q12791
Residue number A
413
Residue number B
487
Peptide name
Calcium-activated potassium channel subunit alpha-1

Ligandability

Cysteine 413 of Calcium-activated potassium channel subunit alpha-1

Cysteine 487 of Calcium-activated potassium channel subunit alpha-1

A redox-regulated disulphide may form within Calcium-activated potassium channel subunit alpha-1 between cysteines 845 and 923 (722 and 800 respectively in this structure).

Details

Redox score ?
66
PDB code
6v5a
Structure name
crystal structure of the human bk channel gating ring l390p mutant
Structure deposition date
2019-12-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
90
Minimum pKa ?
9
% buried
100
Peptide accession
Q12791
Residue number A
845
Residue number B
923
Peptide name
Calcium-activated potassium channel subunit alpha-1

Ligandability

Cysteine 845 of Calcium-activated potassium channel subunit alpha-1

Cysteine 923 of Calcium-activated potassium channel subunit alpha-1

A redox-regulated disulphide may form within Calcium-activated potassium channel subunit alpha-1 between cysteines 693 and 695 (628 and 630 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
6v35
Structure name
cryo-em structure of ca2+-free hsslo1-beta4 channel complex
Structure deposition date
2019-11-25
Thiol separation (Å)
8
Half-sphere exposure sum ?
31
Minimum pKa ?
9
% buried
0
Peptide accession
Q12791
Residue number A
693
Residue number B
695
Peptide name
Calcium-activated potassium channel subunit alpha-1

Ligandability

Cysteine 693 of Calcium-activated potassium channel subunit alpha-1

Cysteine 695 of Calcium-activated potassium channel subunit alpha-1

A redox-regulated disulphide may form within Calcium-activated potassium channel subunit alpha-1 between cysteines 920 and 923 (797 and 800 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
3naf
Structure name
structure of the intracellular gating ring from the human high- conductance ca2+ gated k+ channel (bk channel)
Structure deposition date
2010-06-01
Thiol separation (Å)
5
Half-sphere exposure sum ?
79
Minimum pKa ?
12
% buried
nan
Peptide accession
Q12791
Residue number A
920
Residue number B
923
Peptide name
Calcium-activated potassium channel subunit alpha-1

Ligandability

Cysteine 920 of Calcium-activated potassium channel subunit alpha-1

Cysteine 923 of Calcium-activated potassium channel subunit alpha-1

A redox-regulated disulphide may form within Calcium-activated potassium channel subunit alpha-1 between cysteines 680 and 693 (615 and 628 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
6v35
Structure name
cryo-em structure of ca2+-free hsslo1-beta4 channel complex
Structure deposition date
2019-11-25
Thiol separation (Å)
8
Half-sphere exposure sum ?
33
Minimum pKa ?
9
% buried
0
Peptide accession
Q12791
Residue number A
680
Residue number B
693
Peptide name
Calcium-activated potassium channel subunit alpha-1

Ligandability

Cysteine 680 of Calcium-activated potassium channel subunit alpha-1

Cysteine 693 of Calcium-activated potassium channel subunit alpha-1

A redox-regulated disulphide may form within Calcium-activated potassium channel subunit alpha-1 between cysteines 677 and 693 (612 and 628 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
6v35
Structure name
cryo-em structure of ca2+-free hsslo1-beta4 channel complex
Structure deposition date
2019-11-25
Thiol separation (Å)
8
Half-sphere exposure sum ?
44
Minimum pKa ?
9
% buried
0
Peptide accession
Q12791
Residue number A
677
Residue number B
693
Peptide name
Calcium-activated potassium channel subunit alpha-1

Ligandability

Cysteine 677 of Calcium-activated potassium channel subunit alpha-1

Cysteine 693 of Calcium-activated potassium channel subunit alpha-1

A redox-regulated disulphide may form within Calcium-activated potassium channel subunit alpha-1 between cysteines 1134 and 1174 (1011 and 1051 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
3naf
Structure name
structure of the intracellular gating ring from the human high- conductance ca2+ gated k+ channel (bk channel)
Structure deposition date
2010-06-01
Thiol separation (Å)
6
Half-sphere exposure sum ?
76
Minimum pKa ?
12
% buried
98
Peptide accession
Q12791
Residue number A
1134
Residue number B
1174
Peptide name
Calcium-activated potassium channel subunit alpha-1

Ligandability

Cysteine 1134 of Calcium-activated potassium channel subunit alpha-1

Cysteine 1174 of Calcium-activated potassium channel subunit alpha-1

A redox-regulated disulphide may form within Calcium-activated potassium channel subunit alpha-1 between cysteines 677 and 680 (612 and 615 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
3naf
Structure name
structure of the intracellular gating ring from the human high- conductance ca2+ gated k+ channel (bk channel)
Structure deposition date
2010-06-01
Thiol separation (Å)
9
Half-sphere exposure sum ?
25
Minimum pKa ?
9
% buried
0
Peptide accession
Q12791
Residue number A
677
Residue number B
680
Peptide name
Calcium-activated potassium channel subunit alpha-1

Ligandability

Cysteine 677 of Calcium-activated potassium channel subunit alpha-1

Cysteine 680 of Calcium-activated potassium channel subunit alpha-1

A redox-regulated disulphide may form within Calcium-activated potassium channel subunit alpha-1 between cysteines 1034 and 1151 (911 and 1028 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
6v5a
Structure name
crystal structure of the human bk channel gating ring l390p mutant
Structure deposition date
2019-12-03
Thiol separation (Å)
8
Half-sphere exposure sum ?
59
Minimum pKa ?
8
% buried
65
Peptide accession
Q12791
Residue number A
1034
Residue number B
1151
Peptide name
Calcium-activated potassium channel subunit alpha-1

Ligandability

Cysteine 1034 of Calcium-activated potassium channel subunit alpha-1

Cysteine 1151 of Calcium-activated potassium channel subunit alpha-1

A redox-regulated disulphide may form within Calcium-activated potassium channel subunit alpha-1 between cysteines 1118 and 1124 (995 and 1001 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
6v5a
Structure name
crystal structure of the human bk channel gating ring l390p mutant
Structure deposition date
2019-12-03
Thiol separation (Å)
8
Half-sphere exposure sum ?
55
Minimum pKa ?
10
% buried
29
Peptide accession
Q12791
Residue number A
1118
Residue number B
1124
Peptide name
Calcium-activated potassium channel subunit alpha-1

Ligandability

Cysteine 1118 of Calcium-activated potassium channel subunit alpha-1

Cysteine 1124 of Calcium-activated potassium channel subunit alpha-1

A redox-regulated disulphide may form within Calcium-activated potassium channel subunit alpha-1 between cysteines 619 and 622 (554 and 557 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
6v5a
Structure name
crystal structure of the human bk channel gating ring l390p mutant
Structure deposition date
2019-12-03
Thiol separation (Å)
7
Half-sphere exposure sum ?
81
Minimum pKa ?
12
% buried
100
Peptide accession
Q12791
Residue number A
619
Residue number B
622
Peptide name
Calcium-activated potassium channel subunit alpha-1

Ligandability

Cysteine 619 of Calcium-activated potassium channel subunit alpha-1

Cysteine 622 of Calcium-activated potassium channel subunit alpha-1

A redox-regulated disulphide may form within Calcium-activated potassium channel subunit alpha-1 between cysteines 845 and 920 (722 and 797 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
6v5a
Structure name
crystal structure of the human bk channel gating ring l390p mutant
Structure deposition date
2019-12-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
74
Minimum pKa ?
9
% buried
95
Peptide accession
Q12791
Residue number A
845
Residue number B
920
Peptide name
Calcium-activated potassium channel subunit alpha-1

Ligandability

Cysteine 845 of Calcium-activated potassium channel subunit alpha-1

Cysteine 920 of Calcium-activated potassium channel subunit alpha-1

A redox-regulated disulphide may form within Calcium-activated potassium channel subunit alpha-1 between cysteines 622 and 1124 (557 and 1001 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
6v38
Structure name
cryo-em structure of ca2+-bound hsslo1 channel
Structure deposition date
2019-11-25
Thiol separation (Å)
9
Half-sphere exposure sum ?
56
Minimum pKa ?
10
% buried
60
Peptide accession
Q12791
Residue number A
622
Residue number B
1124
Peptide name
Calcium-activated potassium channel subunit alpha-1

Ligandability

Cysteine 622 of Calcium-activated potassium channel subunit alpha-1

Cysteine 1124 of Calcium-activated potassium channel subunit alpha-1

A redox-regulated disulphide may form within Calcium-activated potassium channel subunit alpha-1 between cysteines 845 and 943 (722 and 820 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
6v5a
Structure name
crystal structure of the human bk channel gating ring l390p mutant
Structure deposition date
2019-12-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
79
Minimum pKa ?
9
% buried
90
Peptide accession
Q12791
Residue number A
845
Residue number B
943
Peptide name
Calcium-activated potassium channel subunit alpha-1

Ligandability

Cysteine 845 of Calcium-activated potassium channel subunit alpha-1

Cysteine 943 of Calcium-activated potassium channel subunit alpha-1

A redox-regulated disulphide may form within Calcium-activated potassium channel subunit alpha-1 between cysteines 619 and 1124 (554 and 1001 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
6v5a
Structure name
crystal structure of the human bk channel gating ring l390p mutant
Structure deposition date
2019-12-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
74
Minimum pKa ?
11
% buried
72
Peptide accession
Q12791
Residue number A
619
Residue number B
1124
Peptide name
Calcium-activated potassium channel subunit alpha-1

Ligandability

Cysteine 619 of Calcium-activated potassium channel subunit alpha-1

Cysteine 1124 of Calcium-activated potassium channel subunit alpha-1

A redox-regulated disulphide may form within Calcium-activated potassium channel subunit alpha-1 between cysteines 563 and 920 (498 and 797 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
6v5a
Structure name
crystal structure of the human bk channel gating ring l390p mutant
Structure deposition date
2019-12-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
72
Minimum pKa ?
12
% buried
95
Peptide accession
Q12791
Residue number A
563
Residue number B
920
Peptide name
Calcium-activated potassium channel subunit alpha-1

Ligandability

Cysteine 563 of Calcium-activated potassium channel subunit alpha-1

Cysteine 920 of Calcium-activated potassium channel subunit alpha-1

A redox-regulated disulphide may form within Calcium-activated potassium channel subunit alpha-1 between cysteines 619 and 1098 (554 and 975 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
6v38
Structure name
cryo-em structure of ca2+-bound hsslo1 channel
Structure deposition date
2019-11-25
Thiol separation (Å)
10
Half-sphere exposure sum ?
69
Minimum pKa ?
11
% buried
63
Peptide accession
Q12791
Residue number A
619
Residue number B
1098
Peptide name
Calcium-activated potassium channel subunit alpha-1

Ligandability

Cysteine 619 of Calcium-activated potassium channel subunit alpha-1

Cysteine 1098 of Calcium-activated potassium channel subunit alpha-1

A redox-regulated disulphide may form within Calcium-activated potassium channel subunit alpha-1 between cysteines 1124 and 1134 (1001 and 1011 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
6v5a
Structure name
crystal structure of the human bk channel gating ring l390p mutant
Structure deposition date
2019-12-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
75
Minimum pKa ?
11
% buried
72
Peptide accession
Q12791
Residue number A
1124
Residue number B
1134
Peptide name
Calcium-activated potassium channel subunit alpha-1

Ligandability

Cysteine 1124 of Calcium-activated potassium channel subunit alpha-1

Cysteine 1134 of Calcium-activated potassium channel subunit alpha-1

A redox-regulated disulphide may form within Calcium-activated potassium channel subunit alpha-1 between cysteines 1098 and 1174 (975 and 1051 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
3naf
Structure name
structure of the intracellular gating ring from the human high- conductance ca2+ gated k+ channel (bk channel)
Structure deposition date
2010-06-01
Thiol separation (Å)
9
Half-sphere exposure sum ?
67
Minimum pKa ?
12
% buried
98
Peptide accession
Q12791
Residue number A
1098
Residue number B
1174
Peptide name
Calcium-activated potassium channel subunit alpha-1

Ligandability

Cysteine 1098 of Calcium-activated potassium channel subunit alpha-1

Cysteine 1174 of Calcium-activated potassium channel subunit alpha-1

A redox-regulated disulphide may form within Calcium-activated potassium channel subunit alpha-1 between cysteines 563 and 923 (498 and 800 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
29
PDB code
3naf
Structure name
structure of the intracellular gating ring from the human high- conductance ca2+ gated k+ channel (bk channel)
Structure deposition date
2010-06-01
Thiol separation (Å)
10
Half-sphere exposure sum ?
90
Minimum pKa ?
12
% buried
nan
Peptide accession
Q12791
Residue number A
563
Residue number B
923
Peptide name
Calcium-activated potassium channel subunit alpha-1

Ligandability

Cysteine 563 of Calcium-activated potassium channel subunit alpha-1

Cysteine 923 of Calcium-activated potassium channel subunit alpha-1

A redox-regulated disulphide may form within Calcium-activated potassium channel subunit alpha-1 between cysteines 619 and 1134 (554 and 1011 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
24
PDB code
6v5a
Structure name
crystal structure of the human bk channel gating ring l390p mutant
Structure deposition date
2019-12-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
91
Minimum pKa ?
13
% buried
100
Peptide accession
Q12791
Residue number A
619
Residue number B
1134
Peptide name
Calcium-activated potassium channel subunit alpha-1

Ligandability

Cysteine 619 of Calcium-activated potassium channel subunit alpha-1

Cysteine 1134 of Calcium-activated potassium channel subunit alpha-1

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