Guanine nucleotide-binding protein subunit beta-5
Intramolecular
Cysteine 171 and cysteine 201
Cysteine 110 and cysteine 153
Cysteine 110 and cysteine 201
Cysteine 114 and cysteine 160
Cysteine 164 and cysteine 171
Cysteine 153 and cysteine 164
Cysteine 153 and cysteine 171
Cysteine 153 and cysteine 201
Cysteine 164 and cysteine 201
Cysteine 219 and cysteine 242
More...Cysteine 147 and cysteine 164
Cysteine 110 and cysteine 164
Cysteine 242 and cysteine 259
Cysteine 153 and cysteine 383
2pbi B 129 B 159
A redox-regulated disulphide may form within Guanine nucleotide-binding protein subunit beta-5 between cysteines 171 and 201 (129 and 159 respectively in this structure).
Details
Redox score ?
68
PDB code
2pbi
Structure name
the multifunctional nature of gbeta5/rgs9 revealed from its crystal structure
Structure deposition date
2007-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
95
Minimum pKa ?
9
% buried
100
Peptide accession
P62881
Residue number A
171
Residue number B
201
Peptide name
Guanine nucleotide-binding protein subunit beta-5
Ligandability
Cysteine 171 of Guanine nucleotide-binding protein subunit beta-5
Cysteine 201 of Guanine nucleotide-binding protein subunit beta-5
2pbi B 68 B 111
A redox-regulated disulphide may form within Guanine nucleotide-binding protein subunit beta-5 between cysteines 110 and 153 (68 and 111 respectively in this structure).
Details
Redox score ?
67
PDB code
2pbi
Structure name
the multifunctional nature of gbeta5/rgs9 revealed from its crystal structure
Structure deposition date
2007-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
98
Minimum pKa ?
7
% buried
100
Peptide accession
P62881
Residue number A
110
Residue number B
153
Peptide name
Guanine nucleotide-binding protein subunit beta-5
Ligandability
Cysteine 110 of Guanine nucleotide-binding protein subunit beta-5
Cysteine 153 of Guanine nucleotide-binding protein subunit beta-5
2pbi B 68 B 159
A redox-regulated disulphide may form within Guanine nucleotide-binding protein subunit beta-5 between cysteines 110 and 201 (68 and 159 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
2pbi
Structure name
the multifunctional nature of gbeta5/rgs9 revealed from its crystal structure
Structure deposition date
2007-03-28
Thiol separation (Å)
7
Half-sphere exposure sum ?
97
Minimum pKa ?
7
% buried
100
Peptide accession
P62881
Residue number A
110
Residue number B
201
Peptide name
Guanine nucleotide-binding protein subunit beta-5
Ligandability
Cysteine 110 of Guanine nucleotide-binding protein subunit beta-5
Cysteine 201 of Guanine nucleotide-binding protein subunit beta-5
2pbi D 72 D 118
A redox-regulated disulphide may form within Guanine nucleotide-binding protein subunit beta-5 between cysteines 114 and 160 (72 and 118 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
2pbi
Structure name
the multifunctional nature of gbeta5/rgs9 revealed from its crystal structure
Structure deposition date
2007-03-28
Thiol separation (Å)
8
Half-sphere exposure sum ?
58
Minimum pKa ?
9
% buried
34
Peptide accession
P62881
Residue number A
114
Residue number B
160
Peptide name
Guanine nucleotide-binding protein subunit beta-5
Ligandability
Cysteine 114 of Guanine nucleotide-binding protein subunit beta-5
Cysteine 160 of Guanine nucleotide-binding protein subunit beta-5
2pbi D 122 D 129
A redox-regulated disulphide may form within Guanine nucleotide-binding protein subunit beta-5 between cysteines 164 and 171 (122 and 129 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
2pbi
Structure name
the multifunctional nature of gbeta5/rgs9 revealed from its crystal structure
Structure deposition date
2007-03-28
Thiol separation (Å)
7
Half-sphere exposure sum ?
107
Minimum pKa ?
10
% buried
100
Peptide accession
P62881
Residue number A
164
Residue number B
171
Peptide name
Guanine nucleotide-binding protein subunit beta-5
Ligandability
Cysteine 164 of Guanine nucleotide-binding protein subunit beta-5
Cysteine 171 of Guanine nucleotide-binding protein subunit beta-5
7ewr D 111 D 122
A redox-regulated disulphide may form within Guanine nucleotide-binding protein subunit beta-5 between cysteines 153 and 164 (111 and 122 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
7ewr
Structure name
cryo-em structure of human gpr158 in complex with rgs7-gbeta5 in a 2:2:2 ratio
Structure deposition date
2021-05-26
Thiol separation (Å)
7
Half-sphere exposure sum ?
102
Minimum pKa ?
12
% buried
97
Peptide accession
O14775
Residue number A
153
Residue number B
164
Peptide name
Guanine nucleotide-binding protein subunit beta-5
Ligandability
Cysteine 153 of Guanine nucleotide-binding protein subunit beta-5
Cysteine 164 of Guanine nucleotide-binding protein subunit beta-5
7ewp D 111 D 129
A redox-regulated disulphide may form within Guanine nucleotide-binding protein subunit beta-5 between cysteines 153 and 171 (111 and 129 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
7ewp
Structure name
cryo-em structure of human gpr158 in complex with rgs7-gbeta5 in a 2:1:1 ratio
Structure deposition date
2021-05-25
Thiol separation (Å)
9
Half-sphere exposure sum ?
89
Minimum pKa ?
8
% buried
100
Peptide accession
O14775
Residue number A
153
Residue number B
171
Peptide name
Guanine nucleotide-binding protein subunit beta-5
Ligandability
Cysteine 153 of Guanine nucleotide-binding protein subunit beta-5
Cysteine 171 of Guanine nucleotide-binding protein subunit beta-5
7ewr F 111 F 159
A redox-regulated disulphide may form within Guanine nucleotide-binding protein subunit beta-5 between cysteines 153 and 201 (111 and 159 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
7ewr
Structure name
cryo-em structure of human gpr158 in complex with rgs7-gbeta5 in a 2:2:2 ratio
Structure deposition date
2021-05-26
Thiol separation (Å)
7
Half-sphere exposure sum ?
87
Minimum pKa ?
15
% buried
100
Peptide accession
O14775
Residue number A
153
Residue number B
201
Peptide name
Guanine nucleotide-binding protein subunit beta-5
Ligandability
Cysteine 153 of Guanine nucleotide-binding protein subunit beta-5
Cysteine 201 of Guanine nucleotide-binding protein subunit beta-5
2pbi D 122 D 159
A redox-regulated disulphide may form within Guanine nucleotide-binding protein subunit beta-5 between cysteines 164 and 201 (122 and 159 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
2pbi
Structure name
the multifunctional nature of gbeta5/rgs9 revealed from its crystal structure
Structure deposition date
2007-03-28
Thiol separation (Å)
7
Half-sphere exposure sum ?
105
Minimum pKa ?
13
% buried
100
Peptide accession
P62881
Residue number A
164
Residue number B
201
Peptide name
Guanine nucleotide-binding protein subunit beta-5
Ligandability
Cysteine 164 of Guanine nucleotide-binding protein subunit beta-5
Cysteine 201 of Guanine nucleotide-binding protein subunit beta-5
7ewr F 177 F 200
A redox-regulated disulphide may form within Guanine nucleotide-binding protein subunit beta-5 between cysteines 219 and 242 (177 and 200 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
36
PDB code
7ewr
Structure name
cryo-em structure of human gpr158 in complex with rgs7-gbeta5 in a 2:2:2 ratio
Structure deposition date
2021-05-26
Thiol separation (Å)
8
Half-sphere exposure sum ?
92
Minimum pKa ?
12
% buried
100
Peptide accession
O14775
Residue number A
219
Residue number B
242
Peptide name
Guanine nucleotide-binding protein subunit beta-5
Ligandability
Cysteine 219 of Guanine nucleotide-binding protein subunit beta-5
Cysteine 242 of Guanine nucleotide-binding protein subunit beta-5
6n9g D 105 D 122
A redox-regulated disulphide may form within Guanine nucleotide-binding protein subunit beta-5 between cysteines 147 and 164 (105 and 122 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
6n9g
Structure name
crystal structure of rgs7-gbeta5 dimer
Structure deposition date
2018-12-03
Thiol separation (Å)
8
Half-sphere exposure sum ?
96
Minimum pKa ?
13
% buried
100
Peptide accession
P62881
Residue number A
147
Residue number B
164
Peptide name
Guanine nucleotide-binding protein subunit beta-5
Ligandability
Cysteine 147 of Guanine nucleotide-binding protein subunit beta-5
Cysteine 164 of Guanine nucleotide-binding protein subunit beta-5
7ewr F 68 F 122
A redox-regulated disulphide may form within Guanine nucleotide-binding protein subunit beta-5 between cysteines 110 and 164 (68 and 122 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
25
PDB code
7ewr
Structure name
cryo-em structure of human gpr158 in complex with rgs7-gbeta5 in a 2:2:2 ratio
Structure deposition date
2021-05-26
Thiol separation (Å)
9
Half-sphere exposure sum ?
103
Minimum pKa ?
11
% buried
97
Peptide accession
O14775
Residue number A
110
Residue number B
164
Peptide name
Guanine nucleotide-binding protein subunit beta-5
Ligandability
Cysteine 110 of Guanine nucleotide-binding protein subunit beta-5
Cysteine 164 of Guanine nucleotide-binding protein subunit beta-5
2pbi D 200 D 217
A redox-regulated disulphide may form within Guanine nucleotide-binding protein subunit beta-5 between cysteines 242 and 259 (200 and 217 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
25
PDB code
2pbi
Structure name
the multifunctional nature of gbeta5/rgs9 revealed from its crystal structure
Structure deposition date
2007-03-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
95
Minimum pKa ?
13
% buried
100
Peptide accession
P62881
Residue number A
242
Residue number B
259
Peptide name
Guanine nucleotide-binding protein subunit beta-5
Ligandability
Cysteine 242 of Guanine nucleotide-binding protein subunit beta-5
Cysteine 259 of Guanine nucleotide-binding protein subunit beta-5
2pbi B 111 B 341
A redox-regulated disulphide may form within Guanine nucleotide-binding protein subunit beta-5 between cysteines 153 and 383 (111 and 341 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
21
PDB code
2pbi
Structure name
the multifunctional nature of gbeta5/rgs9 revealed from its crystal structure
Structure deposition date
2007-03-28
Thiol separation (Å)
10
Half-sphere exposure sum ?
99
Minimum pKa ?
13
% buried
100
Peptide accession
P62881
Residue number A
153
Residue number B
383
Peptide name
Guanine nucleotide-binding protein subunit beta-5
Ligandability
Cysteine 153 of Guanine nucleotide-binding protein subunit beta-5
Cysteine 383 of Guanine nucleotide-binding protein subunit beta-5
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