Ryanodine receptor 2
Intramolecular
Cysteine 131 and cysteine 158
Cysteine 36 and cysteine 65
Cysteine 24 and cysteine 36
Cysteine 131 and cysteine 132
Cysteine 132 and cysteine 158
Cysteine 757 and cysteine 758
Cysteine 47 and cysteine 131
Cysteine 47 and cysteine 132
Cysteine 47 and cysteine 65
Cysteine 24 and cysteine 65
More...Cysteine 758 and cysteine 822
Cysteine 757 and cysteine 822
Cysteine 1164 and cysteine 1205
3im6 A 131 A 158
A redox-regulated disulphide may form within Ryanodine receptor 2 between cysteines 131 and 158.
Details
Redox score ?
68
PDB code
3im6
Structure name
crystal structure of mouse ryanodine receptor 2 mutant v186m
Structure deposition date
2009-08-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
81
Minimum pKa ?
9
% buried
63
Peptide accession
Q9ERN6
Residue number A
131
Residue number B
158
Peptide name
Ryanodine receptor 2
Ligandability
Cysteine 131 of Ryanodine receptor 2
Cysteine 158 of Ryanodine receptor 2
4jkq A 36 A 65
A redox-regulated disulphide may form within Ryanodine receptor 2 between cysteines 36 and 65.
Details
Redox score ?
67
PDB code
4jkq
Structure name
crystal structure of the n-terminal region of the human ryanodine receptor 2
Structure deposition date
2013-03-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
77
Minimum pKa ?
9
% buried
98
Peptide accession
Q92736
Residue number A
36
Residue number B
65
Peptide name
Ryanodine receptor 2
Ligandability
Cysteine 36 of Ryanodine receptor 2
Cysteine 65 of Ryanodine receptor 2
4l4h A 24 A 36
A redox-regulated disulphide may form within Ryanodine receptor 2 between cysteines 24 and 36. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
4l4h
Structure name
crystal structure of mouse ryanodine receptor isoform 2 (ryr2) 1-547
Structure deposition date
2013-06-07
Thiol separation (Å)
8
Half-sphere exposure sum ?
75
Minimum pKa ?
7
% buried
73
Peptide accession
E9Q401
Residue number A
24
Residue number B
36
Peptide name
Ryanodine receptor 2
Ligandability
Cysteine 24 of Ryanodine receptor 2
Cysteine 36 of Ryanodine receptor 2
4jkq A 131 A 132
A redox-regulated disulphide may form within Ryanodine receptor 2 between cysteines 131 and 132. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
4jkq
Structure name
crystal structure of the n-terminal region of the human ryanodine receptor 2
Structure deposition date
2013-03-11
Thiol separation (Å)
8
Half-sphere exposure sum ?
84
Minimum pKa ?
10
% buried
62
Peptide accession
Q92736
Residue number A
131
Residue number B
132
Peptide name
Ryanodine receptor 2
Ligandability
Cysteine 131 of Ryanodine receptor 2
Cysteine 132 of Ryanodine receptor 2
4l4i A 132 A 158
A redox-regulated disulphide may form within Ryanodine receptor 2 between cysteines 132 and 158. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
4l4i
Structure name
crystal structure of mouse ryanodine receptor isoform 2 (ryr2) 1-547 disease mutant r420q
Structure deposition date
2013-06-07
Thiol separation (Å)
10
Half-sphere exposure sum ?
78
Minimum pKa ?
8
% buried
50
Peptide accession
E9Q401
Residue number A
132
Residue number B
158
Peptide name
Ryanodine receptor 2
Ligandability
Cysteine 132 of Ryanodine receptor 2
Cysteine 158 of Ryanodine receptor 2
6j6l A 757 A 758
A redox-regulated disulphide may form within Ryanodine receptor 2 between cysteines 757 and 758. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
6j6l
Structure name
crystal structure of mouse ryanodine receptor 2 spry1 domain (650-844) disease mutant i784f
Structure deposition date
2019-01-15
Thiol separation (Å)
7
Half-sphere exposure sum ?
98
Minimum pKa ?
12
% buried
94
Peptide accession
E9Q401
Residue number A
757
Residue number B
758
Peptide name
Ryanodine receptor 2
Ligandability
Cysteine 757 of Ryanodine receptor 2
Cysteine 758 of Ryanodine receptor 2
4l4i A 47 A 131
A redox-regulated disulphide may form within Ryanodine receptor 2 between cysteines 47 and 131. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
36
PDB code
4l4i
Structure name
crystal structure of mouse ryanodine receptor isoform 2 (ryr2) 1-547 disease mutant r420q
Structure deposition date
2013-06-07
Thiol separation (Å)
8
Half-sphere exposure sum ?
83
Minimum pKa ?
12
% buried
80
Peptide accession
E9Q401
Residue number A
47
Residue number B
131
Peptide name
Ryanodine receptor 2
Ligandability
Cysteine 47 of Ryanodine receptor 2
Cysteine 131 of Ryanodine receptor 2
2mc2 A 47 A 132
A redox-regulated disulphide may form within Ryanodine receptor 2 between cysteines 47 and 132. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
35
PDB code
2mc2
Structure name
x-ray crystallography-solution nmr hybrid structure of mouse ryr2 domain a
Structure deposition date
2013-08-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
83
Minimum pKa ?
10
% buried
88
Peptide accession
E9Q401
Residue number A
47
Residue number B
132
Peptide name
Ryanodine receptor 2
Ligandability
Cysteine 47 of Ryanodine receptor 2
Cysteine 132 of Ryanodine receptor 2
3im5 B 47 B 65
A redox-regulated disulphide may form within Ryanodine receptor 2 between cysteines 47 and 65. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
32
PDB code
3im5
Structure name
crystal structure of mouse ryanodine receptor 2 (residues 1-217)
Structure deposition date
2009-08-09
Thiol separation (Å)
10
Half-sphere exposure sum ?
76
Minimum pKa ?
13
% buried
nan
Peptide accession
Q9ERN6
Residue number A
47
Residue number B
65
Peptide name
Ryanodine receptor 2
Ligandability
Cysteine 47 of Ryanodine receptor 2
Cysteine 65 of Ryanodine receptor 2
2mc2 A 24 A 65
A redox-regulated disulphide may form within Ryanodine receptor 2 between cysteines 24 and 65. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
32
PDB code
2mc2
Structure name
x-ray crystallography-solution nmr hybrid structure of mouse ryr2 domain a
Structure deposition date
2013-08-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
78
Minimum pKa ?
12
% buried
nan
Peptide accession
E9Q401
Residue number A
24
Residue number B
65
Peptide name
Ryanodine receptor 2
Ligandability
Cysteine 24 of Ryanodine receptor 2
Cysteine 65 of Ryanodine receptor 2
6j6l B 758 B 822
A redox-regulated disulphide may form within Ryanodine receptor 2 between cysteines 758 and 822. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
31
PDB code
6j6l
Structure name
crystal structure of mouse ryanodine receptor 2 spry1 domain (650-844) disease mutant i784f
Structure deposition date
2019-01-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
86
Minimum pKa ?
11
% buried
94
Peptide accession
E9Q401
Residue number A
758
Residue number B
822
Peptide name
Ryanodine receptor 2
Ligandability
Cysteine 758 of Ryanodine receptor 2
Cysteine 822 of Ryanodine receptor 2
6j6l B 757 B 822
A redox-regulated disulphide may form within Ryanodine receptor 2 between cysteines 757 and 822. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
29
PDB code
6j6l
Structure name
crystal structure of mouse ryanodine receptor 2 spry1 domain (650-844) disease mutant i784f
Structure deposition date
2019-01-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
90
Minimum pKa ?
13
% buried
100
Peptide accession
E9Q401
Residue number A
757
Residue number B
822
Peptide name
Ryanodine receptor 2
Ligandability
Cysteine 757 of Ryanodine receptor 2
Cysteine 822 of Ryanodine receptor 2
5vsn A 1164 A 1205
A redox-regulated disulphide may form within Ryanodine receptor 2 between cysteines 1164 and 1205. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
28
PDB code
5vsn
Structure name
crystal structure of mouse ryanodine receptor 2 spry2 domain (1080- 1253) disease mutant p1124l
Structure deposition date
2017-05-12
Thiol separation (Å)
9
Half-sphere exposure sum ?
93
Minimum pKa ?
12
% buried
89
Peptide accession
E9Q401
Residue number A
1164
Residue number B
1205
Peptide name
Ryanodine receptor 2
Ligandability
Cysteine 1164 of Ryanodine receptor 2
Cysteine 1205 of Ryanodine receptor 2
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