G-protein coupled receptor 52
Intramolecular
Cysteine 114 and cysteine 193
Cysteine 114 and cysteine 1039
Cysteine 114 and cysteine 339
Cysteine 27 and cysteine 40
Cysteine 1039 and cysteine 339
Cysteine 134 and cysteine 161
Cysteine 336 and cysteine 339
Cysteine 131 and cysteine 161
Cysteine 131 and cysteine 134
Cysteine 134 and cysteine 40
More...Cysteine 114 and cysteine 131
Cysteine 114 and cysteine 40
Cysteine 1009 and cysteine 339
6li0 A 114 A 193
A redox-regulated disulphide may form within G-protein coupled receptor 52 between cysteines 114 and 193.
Details
Redox score ?
86
PDB code
6li0
Structure name
crystal structure of gpr52 in complex with agonist c17
Structure deposition date
2019-12-10
Thiol separation (Å)
2
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9Y2T5
Residue number A
114
Residue number B
193
Peptide name
G-protein coupled receptor 52
Ligandability
Cysteine 114 of G-protein coupled receptor 52
Cysteine 193 of G-protein coupled receptor 52
6li2 A 1006 A 1039
A redox-regulated disulphide may form within G-protein coupled receptor 52 between cysteines 114 and 1039 (1006 and 1039 respectively in this structure).
Details
Redox score ?
86
PDB code
6li2
Structure name
crystal structure of gpr52 ligand free form with rubredoxin fusion
Structure deposition date
2019-12-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
5
% buried
21
Peptide accession
Q9Y2T5
Residue number A
114
Residue number B
1039
Peptide name
G-protein coupled receptor 52
Ligandability
Cysteine 114 of G-protein coupled receptor 52
Cysteine 1039 of G-protein coupled receptor 52
Cysteine 1039 in protein B could not be asigned to a Uniprot residue.
6li2 A 1006 A 1042
A redox-regulated disulphide may form within G-protein coupled receptor 52 between cysteines 114 and 339 (1006 and 1042 respectively in this structure).
Details
Redox score ?
85
PDB code
6li2
Structure name
crystal structure of gpr52 ligand free form with rubredoxin fusion
Structure deposition date
2019-12-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
5
% buried
10
Peptide accession
Q9Y2T5
Residue number A
114
Residue number B
339
Peptide name
G-protein coupled receptor 52
Ligandability
Cysteine 114 of G-protein coupled receptor 52
Cysteine 339 of G-protein coupled receptor 52
6li1 A 27 A 40
A redox-regulated disulphide may form within G-protein coupled receptor 52 between cysteines 27 and 40.
Details
Redox score ?
83
PDB code
6li1
Structure name
crystal structure of gpr52 ligand free form with flavodoxin fusion
Structure deposition date
2019-12-10
Thiol separation (Å)
2
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9Y2T5
Residue number A
27
Residue number B
40
Peptide name
G-protein coupled receptor 52
Ligandability
Cysteine 27 of G-protein coupled receptor 52
Cysteine 40 of G-protein coupled receptor 52
6li2 A 1039 A 1042
A redox-regulated disulphide may form within G-protein coupled receptor 52 between cysteines 1039 and 339 (1039 and 1042 respectively in this structure).
Details
Redox score ?
81
PDB code
6li2
Structure name
crystal structure of gpr52 ligand free form with rubredoxin fusion
Structure deposition date
2019-12-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
8
% buried
11
Peptide accession
Q9Y2T5
Residue number A
1039
Residue number B
339
Peptide name
G-protein coupled receptor 52
Ligandability
Cysteine 1039 of G-protein coupled receptor 52
Cysteine 339 of G-protein coupled receptor 52
Cysteine 1039 in protein A could not be asigned to a Uniprot residue.
6li0 A 134 A 161
A redox-regulated disulphide may form within G-protein coupled receptor 52 between cysteines 134 and 161.
Details
Redox score ?
73
PDB code
6li0
Structure name
crystal structure of gpr52 in complex with agonist c17
Structure deposition date
2019-12-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
7
% buried
74
Peptide accession
Q9Y2T5
Residue number A
134
Residue number B
161
Peptide name
G-protein coupled receptor 52
Ligandability
Cysteine 134 of G-protein coupled receptor 52
Cysteine 161 of G-protein coupled receptor 52
6li1 A 336 A 339
A redox-regulated disulphide may form within G-protein coupled receptor 52 between cysteines 336 and 339.
Details
Redox score ?
71
PDB code
6li1
Structure name
crystal structure of gpr52 ligand free form with flavodoxin fusion
Structure deposition date
2019-12-10
Thiol separation (Å)
6
Half-sphere exposure sum ?
21
Minimum pKa ?
9
% buried
0
Peptide accession
Q9Y2T5
Residue number A
336
Residue number B
339
Peptide name
G-protein coupled receptor 52
Ligandability
Cysteine 336 of G-protein coupled receptor 52
Cysteine 339 of G-protein coupled receptor 52
6li2 A 131 A 161
A redox-regulated disulphide may form within G-protein coupled receptor 52 between cysteines 131 and 161. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
6li2
Structure name
crystal structure of gpr52 ligand free form with rubredoxin fusion
Structure deposition date
2019-12-10
Thiol separation (Å)
8
Half-sphere exposure sum ?
69
Minimum pKa ?
7
% buried
76
Peptide accession
Q9Y2T5
Residue number A
131
Residue number B
161
Peptide name
G-protein coupled receptor 52
Ligandability
Cysteine 131 of G-protein coupled receptor 52
Cysteine 161 of G-protein coupled receptor 52
6li2 A 131 A 134
A redox-regulated disulphide may form within G-protein coupled receptor 52 between cysteines 131 and 134. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
6li2
Structure name
crystal structure of gpr52 ligand free form with rubredoxin fusion
Structure deposition date
2019-12-10
Thiol separation (Å)
7
Half-sphere exposure sum ?
81
Minimum pKa ?
13
% buried
94
Peptide accession
Q9Y2T5
Residue number A
131
Residue number B
134
Peptide name
G-protein coupled receptor 52
Ligandability
Cysteine 131 of G-protein coupled receptor 52
Cysteine 134 of G-protein coupled receptor 52
6li0 A 1093 A 1102
A redox-regulated disulphide may form within G-protein coupled receptor 52 between cysteines 134 and 40 (1093 and 1102 respectively in this structure).
Details
Redox score ?
nan
PDB code
6li0
Structure name
crystal structure of gpr52 in complex with agonist c17
Structure deposition date
2019-12-10
Thiol separation (Å)
7
Half-sphere exposure sum ?
82
Minimum pKa ?
11
% buried
79
Peptide accession
Q9Y2T5
Residue number A
134
Residue number B
40
Peptide name
G-protein coupled receptor 52
Ligandability
Cysteine 134 of G-protein coupled receptor 52
Cysteine 40 of G-protein coupled receptor 52
Uncertain whether structure cysteine 1093 has been assigned to correct residue.
Uncertain whether structure cysteine 1102 has been assigned to correct residue.
6li0 A 1057 A 1090
A redox-regulated disulphide may form within G-protein coupled receptor 52 between cysteines 114 and 131 (1057 and 1090 respectively in this structure).
Details
Redox score ?
nan
PDB code
6li0
Structure name
crystal structure of gpr52 in complex with agonist c17
Structure deposition date
2019-12-10
Thiol separation (Å)
9
Half-sphere exposure sum ?
99
Minimum pKa ?
13
% buried
100
Peptide accession
Q9Y2T5
Residue number A
114
Residue number B
131
Peptide name
G-protein coupled receptor 52
Ligandability
Cysteine 114 of G-protein coupled receptor 52
Cysteine 131 of G-protein coupled receptor 52
Uncertain whether structure cysteine 1057 has been assigned to correct residue.
Uncertain whether structure cysteine 1090 has been assigned to correct residue.
6li0 A 1057 A 1102
A redox-regulated disulphide may form within G-protein coupled receptor 52 between cysteines 114 and 40 (1057 and 1102 respectively in this structure).
Details
Redox score ?
nan
PDB code
6li0
Structure name
crystal structure of gpr52 in complex with agonist c17
Structure deposition date
2019-12-10
Thiol separation (Å)
10
Half-sphere exposure sum ?
86
Minimum pKa ?
12
% buried
86
Peptide accession
Q9Y2T5
Residue number A
114
Residue number B
40
Peptide name
G-protein coupled receptor 52
Ligandability
Cysteine 114 of G-protein coupled receptor 52
Cysteine 40 of G-protein coupled receptor 52
Uncertain whether structure cysteine 1057 has been assigned to correct residue.
Uncertain whether structure cysteine 1102 has been assigned to correct residue.
6li2 A 1009 A 1042
A redox-regulated disulphide may form within G-protein coupled receptor 52 between cysteines 1009 and 339 (1009 and 1042 respectively in this structure).
Details
Redox score ?
nan
PDB code
6li2
Structure name
crystal structure of gpr52 ligand free form with rubredoxin fusion
Structure deposition date
2019-12-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
39
Minimum pKa ?
8
% buried
2
Peptide accession
Q9Y2T5
Residue number A
1009
Residue number B
339
Peptide name
G-protein coupled receptor 52
Ligandability
Cysteine 1009 of G-protein coupled receptor 52
Cysteine 339 of G-protein coupled receptor 52
Cysteine 1009 in protein A could not be asigned to a Uniprot residue.
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