Potassium voltage-gated channel subfamily H member 1
Intramolecular
Cysteine 559 and cysteine 568
Cysteine 575 and cysteine 640
Cysteine 67 and cysteine 128
Cysteine 575 and cysteine 592
Cysteine 592 and cysteine 640
4llo C 559 C 568
A redox-regulated disulphide may form within Potassium voltage-gated channel subfamily H member 1 between cysteines 559 and 568.
Details
Redox score ?
87
PDB code
4llo
Structure name
structure of the eag domain-cnbhd complex of the mouse eag1 channel
Structure deposition date
2013-07-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q60603
Residue number A
559
Residue number B
568
Peptide name
Potassium voltage-gated channel subfamily H member 1
Ligandability
Cysteine 559 of Potassium voltage-gated channel subfamily H member 1
Cysteine 568 of Potassium voltage-gated channel subfamily H member 1
8ep0 C 575 C 640
A redox-regulated disulphide may form within Potassium voltage-gated channel subfamily H member 1 between cysteines 575 and 640.
Details
Redox score ?
78
PDB code
8ep0
Structure name
eag kv channel with voltage sensor in the intermediate conformation
Structure deposition date
2022-10-04
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
7
% buried
60
Peptide accession
Q63472
Residue number A
575
Residue number B
640
Peptide name
Potassium voltage-gated channel subfamily H member 1
Ligandability
Cysteine 575 of Potassium voltage-gated channel subfamily H member 1
Cysteine 640 of Potassium voltage-gated channel subfamily H member 1
5j7e F 67 F 128
A redox-regulated disulphide may form within Potassium voltage-gated channel subfamily H member 1 between cysteines 67 and 128. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
5j7e
Structure name
heag pas domain
Structure deposition date
2016-04-06
Thiol separation (Å)
6
Half-sphere exposure sum ?
82
Minimum pKa ?
12
% buried
100
Peptide accession
O95259
Residue number A
67
Residue number B
128
Peptide name
Potassium voltage-gated channel subfamily H member 1
Ligandability
Cysteine 67 of Potassium voltage-gated channel subfamily H member 1
Cysteine 128 of Potassium voltage-gated channel subfamily H member 1
6pbx C 575 C 592
A redox-regulated disulphide may form within Potassium voltage-gated channel subfamily H member 1 between cysteines 575 and 592. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
6pbx
Structure name
single particle cryo-em structure of the voltage-gated k+ channel eag1 3-13 deletion mutant bound to calmodulin (conformation 2)
Structure deposition date
2019-06-14
Thiol separation (Å)
8
Half-sphere exposure sum ?
76
Minimum pKa ?
12
% buried
95
Peptide accession
Q63472
Residue number A
575
Residue number B
592
Peptide name
Potassium voltage-gated channel subfamily H member 1
Ligandability
Cysteine 575 of Potassium voltage-gated channel subfamily H member 1
Cysteine 592 of Potassium voltage-gated channel subfamily H member 1
6pby E 592 E 640
A redox-regulated disulphide may form within Potassium voltage-gated channel subfamily H member 1 between cysteines 592 and 640. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
6pby
Structure name
single particle cryo-em structure of the voltage-gated k+ channel eag1 3-13 deletion mutant bound to calmodulin (conformation 1)
Structure deposition date
2019-06-14
Thiol separation (Å)
9
Half-sphere exposure sum ?
78
Minimum pKa ?
11
% buried
92
Peptide accession
Q63472
Residue number A
592
Residue number B
640
Peptide name
Potassium voltage-gated channel subfamily H member 1
Ligandability
Cysteine 592 of Potassium voltage-gated channel subfamily H member 1
Cysteine 640 of Potassium voltage-gated channel subfamily H member 1
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