ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Protein dispatched homolog 1

Intramolecular
Cysteine 397 and cysteine 410
Cysteine 863 and cysteine 872
Cysteine 871 and cysteine 887
Cysteine 384 and cysteine 417
Cysteine 829 and cysteine 849
Cysteine 323 and cysteine 367
Cysteine 340 and cysteine 348
Cysteine 293 and cysteine 348
Cysteine 293 and cysteine 349
Cysteine 1129 and cysteine 1133
More...
Cysteine 872 and cysteine 875
Cysteine 863 and cysteine 875
Cysteine 340 and cysteine 349
Cysteine 863 and cysteine 871
Cysteine 681 and cysteine 686
Cysteine 347 and cysteine 348
Cysteine 863 and cysteine 887
Cysteine 410 and cysteine 417
Cysteine 871 and cysteine 875
Cysteine 875 and cysteine 887
Cysteine 871 and cysteine 872
Cysteine 872 and cysteine 887
Cysteine 293 and cysteine 340
Cysteine 686 and cysteine 689
Cysteine 519 and cysteine 691
Cysteine 384 and cysteine 410
Cysteine 1131 and cysteine 1133
Cysteine 196 and cysteine 203
Cysteine 397 and cysteine 417
Cysteine 384 and cysteine 397
Cysteine 1129 and cysteine 1131
A redox-regulated disulphide may form within Protein dispatched homolog 1 between cysteines 397 and 410.

Details

Redox score ?
91
PDB code
7rpi
Structure name
cryo-em structure of murine dispatched 't' conformation
Structure deposition date
2021-08-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q3TDN0
Residue number A
397
Residue number B
410
Peptide name
Protein dispatched homolog 1

Ligandability

Cysteine 397 of Protein dispatched homolog 1

Cysteine 410 of Protein dispatched homolog 1

A redox-regulated disulphide may form within Protein dispatched homolog 1 between cysteines 863 and 872.

Details

Redox score ?
86
PDB code
7rpj
Structure name
cryo-em structure of murine dispatched nnn mutant
Structure deposition date
2021-08-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
45
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q3TDN0
Residue number A
863
Residue number B
872
Peptide name
Protein dispatched homolog 1

Ligandability

Cysteine 863 of Protein dispatched homolog 1

Cysteine 872 of Protein dispatched homolog 1

A redox-regulated disulphide may form within Protein dispatched homolog 1 between cysteines 871 and 887.

Details

Redox score ?
84
PDB code
7rph
Structure name
cryo-em structure of murine dispatched 'r' conformation
Structure deposition date
2021-08-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q3TDN0
Residue number A
871
Residue number B
887
Peptide name
Protein dispatched homolog 1

Ligandability

Cysteine 871 of Protein dispatched homolog 1

Cysteine 887 of Protein dispatched homolog 1

A redox-regulated disulphide may form within Protein dispatched homolog 1 between cysteines 384 and 417.

Details

Redox score ?
83
PDB code
7rpj
Structure name
cryo-em structure of murine dispatched nnn mutant
Structure deposition date
2021-08-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q3TDN0
Residue number A
384
Residue number B
417
Peptide name
Protein dispatched homolog 1

Ligandability

Cysteine 384 of Protein dispatched homolog 1

Cysteine 417 of Protein dispatched homolog 1

A redox-regulated disulphide may form within Protein dispatched homolog 1 between cysteines 829 and 849.

Details

Redox score ?
82
PDB code
7rph
Structure name
cryo-em structure of murine dispatched 'r' conformation
Structure deposition date
2021-08-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q3TDN0
Residue number A
829
Residue number B
849
Peptide name
Protein dispatched homolog 1

Ligandability

Cysteine 829 of Protein dispatched homolog 1

Cysteine 849 of Protein dispatched homolog 1

A redox-regulated disulphide may form within Protein dispatched homolog 1 between cysteines 323 and 367.

Details

Redox score ?
77
PDB code
7e2h
Structure name
cryo-em structure of hdisp1nnn-3c-cleavage
Structure deposition date
2021-02-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
72
Minimum pKa ?
7
% buried
76
Peptide accession
Q96F81
Residue number A
323
Residue number B
367
Peptide name
Protein dispatched homolog 1

Ligandability

Cysteine 323 of Protein dispatched homolog 1

Cysteine 367 of Protein dispatched homolog 1

A redox-regulated disulphide may form within Protein dispatched homolog 1 between cysteines 340 and 348.

Details

Redox score ?
70
PDB code
7e2g
Structure name
cryo-em structure of hdisp1nnn-3c
Structure deposition date
2021-02-05
Thiol separation (Å)
5
Half-sphere exposure sum ?
46
Minimum pKa ?
9
% buried
10
Peptide accession
Q96F81
Residue number A
340
Residue number B
348
Peptide name
Protein dispatched homolog 1

Ligandability

Cysteine 340 of Protein dispatched homolog 1

Cysteine 348 of Protein dispatched homolog 1

A redox-regulated disulphide may form within Protein dispatched homolog 1 between cysteines 293 and 348.

Details

Redox score ?
66
PDB code
7e2h
Structure name
cryo-em structure of hdisp1nnn-3c-cleavage
Structure deposition date
2021-02-05
Thiol separation (Å)
6
Half-sphere exposure sum ?
55
Minimum pKa ?
9
% buried
24
Peptide accession
Q96F81
Residue number A
293
Residue number B
348
Peptide name
Protein dispatched homolog 1

Ligandability

Cysteine 293 of Protein dispatched homolog 1

Cysteine 348 of Protein dispatched homolog 1

A redox-regulated disulphide may form within Protein dispatched homolog 1 between cysteines 293 and 349.

Details

Redox score ?
64
PDB code
7e2i
Structure name
cryo-em structure of hdisp1nnn-shhn
Structure deposition date
2021-02-05
Thiol separation (Å)
5
Half-sphere exposure sum ?
59
Minimum pKa ?
8
% buried
82
Peptide accession
Q96F81
Residue number A
293
Residue number B
349
Peptide name
Protein dispatched homolog 1

Ligandability

Cysteine 293 of Protein dispatched homolog 1

Cysteine 349 of Protein dispatched homolog 1

A redox-regulated disulphide may form within Protein dispatched homolog 1 between cysteines 1129 and 1133.

Details

Redox score ?
62
PDB code
7e2i
Structure name
cryo-em structure of hdisp1nnn-shhn
Structure deposition date
2021-02-05
Thiol separation (Å)
5
Half-sphere exposure sum ?
63
Minimum pKa ?
10
% buried
40
Peptide accession
Q96F81
Residue number A
1129
Residue number B
1133
Peptide name
Protein dispatched homolog 1

Ligandability

Cysteine 1129 of Protein dispatched homolog 1

Cysteine 1133 of Protein dispatched homolog 1

A redox-regulated disulphide may form within Protein dispatched homolog 1 between cysteines 872 and 875.

Details

Redox score ?
62
PDB code
7rph
Structure name
cryo-em structure of murine dispatched 'r' conformation
Structure deposition date
2021-08-03
Thiol separation (Å)
6
Half-sphere exposure sum ?
49
Minimum pKa ?
10
% buried
nan
Peptide accession
Q3TDN0
Residue number A
872
Residue number B
875
Peptide name
Protein dispatched homolog 1

Ligandability

Cysteine 872 of Protein dispatched homolog 1

Cysteine 875 of Protein dispatched homolog 1

A redox-regulated disulphide may form within Protein dispatched homolog 1 between cysteines 863 and 875. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
7rph
Structure name
cryo-em structure of murine dispatched 'r' conformation
Structure deposition date
2021-08-03
Thiol separation (Å)
7
Half-sphere exposure sum ?
40
Minimum pKa ?
10
% buried
nan
Peptide accession
Q3TDN0
Residue number A
863
Residue number B
875
Peptide name
Protein dispatched homolog 1

Ligandability

Cysteine 863 of Protein dispatched homolog 1

Cysteine 875 of Protein dispatched homolog 1

A redox-regulated disulphide may form within Protein dispatched homolog 1 between cysteines 340 and 349. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
7e2g
Structure name
cryo-em structure of hdisp1nnn-3c
Structure deposition date
2021-02-05
Thiol separation (Å)
7
Half-sphere exposure sum ?
53
Minimum pKa ?
10
% buried
18
Peptide accession
Q96F81
Residue number A
340
Residue number B
349
Peptide name
Protein dispatched homolog 1

Ligandability

Cysteine 340 of Protein dispatched homolog 1

Cysteine 349 of Protein dispatched homolog 1

A redox-regulated disulphide may form within Protein dispatched homolog 1 between cysteines 863 and 871. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
7rpj
Structure name
cryo-em structure of murine dispatched nnn mutant
Structure deposition date
2021-08-03
Thiol separation (Å)
7
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q3TDN0
Residue number A
863
Residue number B
871
Peptide name
Protein dispatched homolog 1

Ligandability

Cysteine 863 of Protein dispatched homolog 1

Cysteine 871 of Protein dispatched homolog 1

A redox-regulated disulphide may form within Protein dispatched homolog 1 between cysteines 681 and 686. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
7rpi
Structure name
cryo-em structure of murine dispatched 't' conformation
Structure deposition date
2021-08-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
nan
Minimum pKa ?
9
% buried
0
Peptide accession
Q3TDN0
Residue number A
681
Residue number B
686
Peptide name
Protein dispatched homolog 1

Ligandability

Cysteine 681 of Protein dispatched homolog 1

Cysteine 686 of Protein dispatched homolog 1

A redox-regulated disulphide may form within Protein dispatched homolog 1 between cysteines 347 and 348. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
7rpi
Structure name
cryo-em structure of murine dispatched 't' conformation
Structure deposition date
2021-08-03
Thiol separation (Å)
7
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q3TDN0
Residue number A
347
Residue number B
348
Peptide name
Protein dispatched homolog 1

Ligandability

Cysteine 347 of Protein dispatched homolog 1

Cysteine 348 of Protein dispatched homolog 1

A redox-regulated disulphide may form within Protein dispatched homolog 1 between cysteines 863 and 887. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
7rpj
Structure name
cryo-em structure of murine dispatched nnn mutant
Structure deposition date
2021-08-03
Thiol separation (Å)
8
Half-sphere exposure sum ?
47
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q3TDN0
Residue number A
863
Residue number B
887
Peptide name
Protein dispatched homolog 1

Ligandability

Cysteine 863 of Protein dispatched homolog 1

Cysteine 887 of Protein dispatched homolog 1

A redox-regulated disulphide may form within Protein dispatched homolog 1 between cysteines 410 and 417. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
7rph
Structure name
cryo-em structure of murine dispatched 'r' conformation
Structure deposition date
2021-08-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q3TDN0
Residue number A
410
Residue number B
417
Peptide name
Protein dispatched homolog 1

Ligandability

Cysteine 410 of Protein dispatched homolog 1

Cysteine 417 of Protein dispatched homolog 1

A redox-regulated disulphide may form within Protein dispatched homolog 1 between cysteines 871 and 875. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
7rpi
Structure name
cryo-em structure of murine dispatched 't' conformation
Structure deposition date
2021-08-03
Thiol separation (Å)
8
Half-sphere exposure sum ?
59
Minimum pKa ?
9
% buried
nan
Peptide accession
Q3TDN0
Residue number A
871
Residue number B
875
Peptide name
Protein dispatched homolog 1

Ligandability

Cysteine 871 of Protein dispatched homolog 1

Cysteine 875 of Protein dispatched homolog 1

A redox-regulated disulphide may form within Protein dispatched homolog 1 between cysteines 875 and 887. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
7rpj
Structure name
cryo-em structure of murine dispatched nnn mutant
Structure deposition date
2021-08-03
Thiol separation (Å)
8
Half-sphere exposure sum ?
52
Minimum pKa ?
9
% buried
nan
Peptide accession
Q3TDN0
Residue number A
875
Residue number B
887
Peptide name
Protein dispatched homolog 1

Ligandability

Cysteine 875 of Protein dispatched homolog 1

Cysteine 887 of Protein dispatched homolog 1

A redox-regulated disulphide may form within Protein dispatched homolog 1 between cysteines 871 and 872. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
7rph
Structure name
cryo-em structure of murine dispatched 'r' conformation
Structure deposition date
2021-08-03
Thiol separation (Å)
8
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q3TDN0
Residue number A
871
Residue number B
872
Peptide name
Protein dispatched homolog 1

Ligandability

Cysteine 871 of Protein dispatched homolog 1

Cysteine 872 of Protein dispatched homolog 1

A redox-regulated disulphide may form within Protein dispatched homolog 1 between cysteines 872 and 887. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
7rpj
Structure name
cryo-em structure of murine dispatched nnn mutant
Structure deposition date
2021-08-03
Thiol separation (Å)
8
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q3TDN0
Residue number A
872
Residue number B
887
Peptide name
Protein dispatched homolog 1

Ligandability

Cysteine 872 of Protein dispatched homolog 1

Cysteine 887 of Protein dispatched homolog 1

A redox-regulated disulphide may form within Protein dispatched homolog 1 between cysteines 293 and 340. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
7e2i
Structure name
cryo-em structure of hdisp1nnn-shhn
Structure deposition date
2021-02-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
57
Minimum pKa ?
8
% buried
52
Peptide accession
Q96F81
Residue number A
293
Residue number B
340
Peptide name
Protein dispatched homolog 1

Ligandability

Cysteine 293 of Protein dispatched homolog 1

Cysteine 340 of Protein dispatched homolog 1

A redox-regulated disulphide may form within Protein dispatched homolog 1 between cysteines 686 and 689. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
7rpk
Structure name
cryo-em structure of murine dispatched in complex with sonic hedgehog
Structure deposition date
2021-08-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
30
Minimum pKa ?
9
% buried
2
Peptide accession
Q3TDN0
Residue number A
686
Residue number B
689
Peptide name
Protein dispatched homolog 1

Ligandability

Cysteine 686 of Protein dispatched homolog 1

Cysteine 689 of Protein dispatched homolog 1

A redox-regulated disulphide may form within Protein dispatched homolog 1 between cysteines 519 and 691. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
7e2g
Structure name
cryo-em structure of hdisp1nnn-3c
Structure deposition date
2021-02-05
Thiol separation (Å)
10
Half-sphere exposure sum ?
35
Minimum pKa ?
9
% buried
2
Peptide accession
Q96F81
Residue number A
519
Residue number B
691
Peptide name
Protein dispatched homolog 1

Ligandability

Cysteine 519 of Protein dispatched homolog 1

Cysteine 691 of Protein dispatched homolog 1

A redox-regulated disulphide may form within Protein dispatched homolog 1 between cysteines 384 and 410. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
7rpi
Structure name
cryo-em structure of murine dispatched 't' conformation
Structure deposition date
2021-08-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q3TDN0
Residue number A
384
Residue number B
410
Peptide name
Protein dispatched homolog 1

Ligandability

Cysteine 384 of Protein dispatched homolog 1

Cysteine 410 of Protein dispatched homolog 1

A redox-regulated disulphide may form within Protein dispatched homolog 1 between cysteines 1131 and 1133. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
6xe6
Structure name
structure of human dispatched-1 (disp1)
Structure deposition date
2020-06-12
Thiol separation (Å)
9
Half-sphere exposure sum ?
57
Minimum pKa ?
9
% buried
50
Peptide accession
Q96F81
Residue number A
1131
Residue number B
1133
Peptide name
Protein dispatched homolog 1

Ligandability

Cysteine 1131 of Protein dispatched homolog 1

Cysteine 1133 of Protein dispatched homolog 1

A redox-regulated disulphide may form within Protein dispatched homolog 1 between cysteines 196 and 203. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
6xe6
Structure name
structure of human dispatched-1 (disp1)
Structure deposition date
2020-06-12
Thiol separation (Å)
9
Half-sphere exposure sum ?
52
Minimum pKa ?
11
% buried
38
Peptide accession
Q96F81
Residue number A
196
Residue number B
203
Peptide name
Protein dispatched homolog 1

Ligandability

Cysteine 196 of Protein dispatched homolog 1

Cysteine 203 of Protein dispatched homolog 1

A redox-regulated disulphide may form within Protein dispatched homolog 1 between cysteines 397 and 417. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
7rpi
Structure name
cryo-em structure of murine dispatched 't' conformation
Structure deposition date
2021-08-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q3TDN0
Residue number A
397
Residue number B
417
Peptide name
Protein dispatched homolog 1

Ligandability

Cysteine 397 of Protein dispatched homolog 1

Cysteine 417 of Protein dispatched homolog 1

A redox-regulated disulphide may form within Protein dispatched homolog 1 between cysteines 384 and 397. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
7rph
Structure name
cryo-em structure of murine dispatched 'r' conformation
Structure deposition date
2021-08-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q3TDN0
Residue number A
384
Residue number B
397
Peptide name
Protein dispatched homolog 1

Ligandability

Cysteine 384 of Protein dispatched homolog 1

Cysteine 397 of Protein dispatched homolog 1

A redox-regulated disulphide may form within Protein dispatched homolog 1 between cysteines 1129 and 1131. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
6xe6
Structure name
structure of human dispatched-1 (disp1)
Structure deposition date
2020-06-12
Thiol separation (Å)
10
Half-sphere exposure sum ?
72
Minimum pKa ?
11
% buried
73
Peptide accession
Q96F81
Residue number A
1129
Residue number B
1131
Peptide name
Protein dispatched homolog 1

Ligandability

Cysteine 1129 of Protein dispatched homolog 1

Cysteine 1131 of Protein dispatched homolog 1

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