ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Smoothened homolog

Intramolecular
Cysteine 494 and cysteine 511
Cysteine 64 and cysteine 178
Cysteine 70 and cysteine 134
Cysteine 147 and cysteine 169
Cysteine 193 and cysteine 213
Cysteine 122 and cysteine 158
Cysteine 221 and cysteine 299
Cysteine 78 and cysteine 127
Cysteine 314 and cysteine 390
Cysteine 217 and cysteine 390
More...
Cysteine 295 and cysteine 390
Cysteine 217 and cysteine 314
Cysteine 295 and cysteine 314
Cysteine 118 and cysteine 213
Cysteine 82 and cysteine 687
Cysteine 64 and cysteine 469
Cysteine 1057 and cysteine 78
Cysteine 1093 and cysteine 1102
Cysteine 1057 and cysteine 1102
A redox-regulated disulphide may form within Smoothened homolog between cysteines 494 and 511.

Details

Redox score ?
87
PDB code
6o3c
Structure name
crystal structure of active smoothened bound to sag21k, cholesterol, and nbsmo8
Structure deposition date
2019-02-26
Thiol separation (Å)
2
Half-sphere exposure sum ?
42
Minimum pKa ?
nan
% buried
nan
Peptide accession
P56726
Residue number A
494
Residue number B
511
Peptide name
Smoothened homolog

Ligandability

Cysteine 494 of Smoothened homolog

Cysteine 511 of Smoothened homolog

A redox-regulated disulphide may form within Smoothened homolog between cysteines 64 and 178.

Details

Redox score ?
87
PDB code
5l7d
Structure name
structure of human smoothened in complex with cholesterol
Structure deposition date
2016-06-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q99835
Residue number A
64
Residue number B
178
Peptide name
Smoothened homolog

Ligandability

Cysteine 64 of Smoothened homolog

Cysteine 178 of Smoothened homolog

A redox-regulated disulphide may form within Smoothened homolog between cysteines 70 and 134.

Details

Redox score ?
86
PDB code
5l7i
Structure name
structure of human smoothened in complex with vismodegib
Structure deposition date
2016-06-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q99835
Residue number A
70
Residue number B
134
Peptide name
Smoothened homolog

Ligandability

Cysteine 70 of Smoothened homolog

Cysteine 134 of Smoothened homolog

A redox-regulated disulphide may form within Smoothened homolog between cysteines 147 and 169.

Details

Redox score ?
85
PDB code
5l7i
Structure name
structure of human smoothened in complex with vismodegib
Structure deposition date
2016-06-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q99835
Residue number A
147
Residue number B
169
Peptide name
Smoothened homolog

Ligandability

Cysteine 147 of Smoothened homolog

Cysteine 169 of Smoothened homolog

A redox-regulated disulphide may form within Smoothened homolog between cysteines 193 and 213.

Details

Redox score ?
83
PDB code
5v57
Structure name
3
Structure deposition date
2017-03-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q99835
Residue number A
193
Residue number B
213
Peptide name
Smoothened homolog

Ligandability

Cysteine 193 of Smoothened homolog

Cysteine 213 of Smoothened homolog

A redox-regulated disulphide may form within Smoothened homolog between cysteines 122 and 158.

Details

Redox score ?
82
PDB code
6o3c
Structure name
crystal structure of active smoothened bound to sag21k, cholesterol, and nbsmo8
Structure deposition date
2019-02-26
Thiol separation (Å)
2
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P56726
Residue number A
122
Residue number B
158
Peptide name
Smoothened homolog

Ligandability

Cysteine 122 of Smoothened homolog

Cysteine 158 of Smoothened homolog

A redox-regulated disulphide may form within Smoothened homolog between cysteines 221 and 299.

Details

Redox score ?
81
PDB code
6o3c
Structure name
crystal structure of active smoothened bound to sag21k, cholesterol, and nbsmo8
Structure deposition date
2019-02-26
Thiol separation (Å)
2
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
P56726
Residue number A
221
Residue number B
299
Peptide name
Smoothened homolog

Ligandability

Cysteine 221 of Smoothened homolog

Cysteine 299 of Smoothened homolog

A redox-regulated disulphide may form within Smoothened homolog between cysteines 78 and 127.

Details

Redox score ?
81
PDB code
5v57
Structure name
3
Structure deposition date
2017-03-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q99835
Residue number A
78
Residue number B
127
Peptide name
Smoothened homolog

Ligandability

Cysteine 78 of Smoothened homolog

Cysteine 127 of Smoothened homolog

A redox-regulated disulphide may form within Smoothened homolog between cysteines 314 and 390.

Details

Redox score ?
62
PDB code
6ot0
Structure name
structure of human smoothened-gi complex
Structure deposition date
2019-05-02
Thiol separation (Å)
5
Half-sphere exposure sum ?
76
Minimum pKa ?
10
% buried
66
Peptide accession
Q99835
Residue number A
314
Residue number B
390
Peptide name
Smoothened homolog

Ligandability

Cysteine 314 of Smoothened homolog

Cysteine 390 of Smoothened homolog

A redox-regulated disulphide may form within Smoothened homolog between cysteines 217 and 390. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
4jkv
Structure name
structure of the human smoothened 7tm receptor in complex with an antitumor agent
Structure deposition date
2013-03-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
84
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q99835
Residue number A
217
Residue number B
390
Peptide name
Smoothened homolog

Ligandability

Cysteine 217 of Smoothened homolog

Cysteine 390 of Smoothened homolog

A redox-regulated disulphide may form within Smoothened homolog between cysteines 295 and 390. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
4jkv
Structure name
structure of the human smoothened 7tm receptor in complex with an antitumor agent
Structure deposition date
2013-03-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
86
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q99835
Residue number A
295
Residue number B
390
Peptide name
Smoothened homolog

Ligandability

Cysteine 295 of Smoothened homolog

Cysteine 390 of Smoothened homolog

A redox-regulated disulphide may form within Smoothened homolog between cysteines 217 and 314. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
4jkv
Structure name
structure of the human smoothened 7tm receptor in complex with an antitumor agent
Structure deposition date
2013-03-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q99835
Residue number A
217
Residue number B
314
Peptide name
Smoothened homolog

Ligandability

Cysteine 217 of Smoothened homolog

Cysteine 314 of Smoothened homolog

A redox-regulated disulphide may form within Smoothened homolog between cysteines 295 and 314. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
4jkv
Structure name
structure of the human smoothened 7tm receptor in complex with an antitumor agent
Structure deposition date
2013-03-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q99835
Residue number A
295
Residue number B
314
Peptide name
Smoothened homolog

Ligandability

Cysteine 295 of Smoothened homolog

Cysteine 314 of Smoothened homolog

A redox-regulated disulphide may form within Smoothened homolog between cysteines 118 and 213. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
6xbj
Structure name
structure of human smo-d384r complex with gi
Structure deposition date
2020-06-06
Thiol separation (Å)
10
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q99835
Residue number A
118
Residue number B
213
Peptide name
Smoothened homolog

Ligandability

Cysteine 118 of Smoothened homolog

Cysteine 213 of Smoothened homolog

A redox-regulated disulphide may form within Smoothened homolog between cysteines 82 and 687 (1133 and 1188 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
8cxo
Structure name
cryo-em structure of the unliganded msmo-pgs2 in a lipidic environment
Structure deposition date
2022-05-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
75
Minimum pKa ?
12
% buried
84
Peptide accession
P56726
Residue number A
82
Residue number B
687
Peptide name
Smoothened homolog

Ligandability

Cysteine 82 of Smoothened homolog

Cysteine 687 of Smoothened homolog

A redox-regulated disulphide may form within Smoothened homolog between cysteines 64 and 469 (111 and 496 respectively in this structure).

Details

Redox score ?
nan
PDB code
6xbk
Structure name
structure of human smo-g111c/i496c complex with gi
Structure deposition date
2020-06-06
Thiol separation (Å)
2
Half-sphere exposure sum ?
43
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q99835
Residue number A
64
Residue number B
469
Peptide name
Smoothened homolog

Ligandability

Cysteine 64 of Smoothened homolog

Cysteine 469 of Smoothened homolog

Uncertain whether structure cysteine 496 has been assigned to correct residue.
A redox-regulated disulphide may form within Smoothened homolog between cysteines 1057 and 78 (1057 and 1090 respectively in this structure).

Details

Redox score ?
nan
PDB code
5v56
Structure name
2
Structure deposition date
2017-03-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
99
Minimum pKa ?
13
% buried
100
Peptide accession
Q99835
Residue number A
1057
Residue number B
78
Peptide name
Smoothened homolog

Ligandability

Cysteine 1057 of Smoothened homolog

Cysteine 78 of Smoothened homolog

Cysteine 1057 in protein A could not be asigned to a Uniprot residue.
Uncertain whether structure cysteine 1090 has been assigned to correct residue.
A redox-regulated disulphide may form within Smoothened homolog between cysteines 1093 and 1102.

Details

Redox score ?
nan
PDB code
5v57
Structure name
3
Structure deposition date
2017-03-13
Thiol separation (Å)
7
Half-sphere exposure sum ?
82
Minimum pKa ?
12
% buried
79
Peptide accession
Q99835
Residue number A
1093
Residue number B
1102
Peptide name
Smoothened homolog

Ligandability

Cysteine 1093 of Smoothened homolog

Cysteine 1102 of Smoothened homolog

Cysteine 1093 in protein A could not be asigned to a Uniprot residue.
Cysteine 1102 in protein B could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within Smoothened homolog between cysteines 1057 and 1102.

Details

Redox score ?
nan
PDB code
5v57
Structure name
3
Structure deposition date
2017-03-13
Thiol separation (Å)
10
Half-sphere exposure sum ?
88
Minimum pKa ?
12
% buried
86
Peptide accession
Q99835
Residue number A
1057
Residue number B
1102
Peptide name
Smoothened homolog

Ligandability

Cysteine 1057 of Smoothened homolog

Cysteine 1102 of Smoothened homolog

Cysteine 1057 in protein A could not be asigned to a Uniprot residue.
Cysteine 1102 in protein B could not be asigned to a Uniprot residue.
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