ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Sortilin

Intramolecular
Cysteine 53 and cysteine 554
Cysteine 668 and cysteine 723
Cysteine 448 and cysteine 458
Cysteine 634 and cysteine 666
Cysteine 612 and cysteine 651 L
Cysteine 675 and cysteine 688
Cysteine 702 and cysteine 740 L
Cysteine 257 and cysteine 277
Cysteine 86 and cysteine 556
Cysteine 666 and cysteine 668
More...
Cysteine 666 and cysteine 723
Cysteine 634 and cysteine 723
Cysteine 632 and cysteine 666
Cysteine 702 and cysteine 707 L
A redox-regulated disulphide may form within Sortilin between cysteines 53 and 554 (53 and 523 respectively in this structure).

Details

Redox score ?
87
PDB code
5nnj
Structure name
dimer structure of sortilin ectodomain crystal form 3, 4
Structure deposition date
2017-04-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6PHU5
Residue number A
53
Residue number B
554
Peptide name
Sortilin

Ligandability

Cysteine 53 of Sortilin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 554 of Sortilin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 53 in protein A could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within Sortilin between cysteines 668 and 723 (635 and 690 respectively in this structure).

Details

Redox score ?
87
PDB code
6eho
Structure name
dimer of the sortilin vps10p domain at low ph
Structure deposition date
2017-09-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q99523
Residue number A
668
Residue number B
723
Peptide name
Sortilin

Ligandability

Cysteine 668 of Sortilin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 723 of Sortilin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Sortilin between cysteines 448 and 458 (415 and 425 respectively in this structure).

Details

Redox score ?
86
PDB code
4po7
Structure name
structure of the sortilin:neurotensin complex at excess neurotensin concentration
Structure deposition date
2014-02-25
Thiol separation (Å)
2
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q99523
Residue number A
448
Residue number B
458
Peptide name
Sortilin

Ligandability

Cysteine 448 of Sortilin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 458 of Sortilin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Sortilin between cysteines 634 and 666 (601 and 633 respectively in this structure).

Details

Redox score ?
84
PDB code
6eho
Structure name
dimer of the sortilin vps10p domain at low ph
Structure deposition date
2017-09-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q99523
Residue number A
634
Residue number B
666
Peptide name
Sortilin

Ligandability

Cysteine 634 of Sortilin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 666 of Sortilin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Sortilin between cysteines 612 and 651 (579 and 618 respectively in this structure).

Details

Redox score ?
83
PDB code
4msl
Structure name
crystal structure of the vps10p domain of human sortilin/nts3 in complex with af40431
Structure deposition date
2013-09-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q99523
Residue number A
612
Residue number B
651
Peptide name
Sortilin

Ligandability

Cysteine 612 of Sortilin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 651 of Sortilin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Sortilin between cysteines 675 and 688 (642 and 655 respectively in this structure).

Details

Redox score ?
83
PDB code
6x4h
Structure name
sortilin-progranulin interaction with compound 24
Structure deposition date
2020-05-22
Thiol separation (Å)
3
Half-sphere exposure sum ?
60
Minimum pKa ?
7
% buried
54
Peptide accession
Q99523
Residue number A
675
Residue number B
688
Peptide name
Sortilin

Ligandability

Cysteine 675 of Sortilin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 688 of Sortilin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Sortilin between cysteines 702 and 740 (669 and 707 respectively in this structure).

Details

Redox score ?
79
PDB code
6x4h
Structure name
sortilin-progranulin interaction with compound 24
Structure deposition date
2020-05-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
9
% buried
29
Peptide accession
Q99523
Residue number A
702
Residue number B
740
Peptide name
Sortilin

Ligandability

Cysteine 702 of Sortilin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

Cysteine 740 of Sortilin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Sortilin between cysteines 257 and 277 (224 and 244 respectively in this structure).

Details

Redox score ?
78
PDB code
6x48
Structure name
sortilin-progranulin interaction with compound 17
Structure deposition date
2020-05-22
Thiol separation (Å)
3
Half-sphere exposure sum ?
64
Minimum pKa ?
9
% buried
34
Peptide accession
Q99523
Residue number A
257
Residue number B
277
Peptide name
Sortilin

Ligandability

Cysteine 257 of Sortilin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 277 of Sortilin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Sortilin between cysteines 86 and 556 (53 and 523 respectively in this structure).

Details

Redox score ?
78
PDB code
6x3l
Structure name
sortilin-progranulin interaction with compound 2
Structure deposition date
2020-05-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
nan
Minimum pKa ?
9
% buried
nan
Peptide accession
Q99523
Residue number A
86
Residue number B
556
Peptide name
Sortilin

Ligandability

Cysteine 86 of Sortilin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 556 of Sortilin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Sortilin between cysteines 666 and 668 (633 and 635 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
6x48
Structure name
sortilin-progranulin interaction with compound 17
Structure deposition date
2020-05-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
51
Minimum pKa ?
9
% buried
21
Peptide accession
Q99523
Residue number A
666
Residue number B
668
Peptide name
Sortilin

Ligandability

Cysteine 666 of Sortilin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 668 of Sortilin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Sortilin between cysteines 666 and 723 (633 and 690 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
6eho
Structure name
dimer of the sortilin vps10p domain at low ph
Structure deposition date
2017-09-14
Thiol separation (Å)
8
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q99523
Residue number A
666
Residue number B
723
Peptide name
Sortilin

Ligandability

Cysteine 666 of Sortilin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 723 of Sortilin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Sortilin between cysteines 634 and 723 (601 and 690 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
6x3l
Structure name
sortilin-progranulin interaction with compound 2
Structure deposition date
2020-05-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
65
Minimum pKa ?
13
% buried
nan
Peptide accession
Q99523
Residue number A
634
Residue number B
723
Peptide name
Sortilin

Ligandability

Cysteine 634 of Sortilin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 723 of Sortilin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Sortilin between cysteines 632 and 666 (601 and 635 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
5nni
Structure name
dimer structure of sortilin ectodomain crystal form 2, 3
Structure deposition date
2017-04-09
Thiol separation (Å)
10
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6PHU5
Residue number A
632
Residue number B
666
Peptide name
Sortilin

Ligandability

Cysteine 632 of Sortilin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 666 of Sortilin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Sortilin between cysteines 702 and 707 (669 and 707 respectively in this structure).

Details

Redox score ?
nan
PDB code
6eho
Structure name
dimer of the sortilin vps10p domain at low ph
Structure deposition date
2017-09-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q99523
Residue number A
702
Residue number B
707
Peptide name
Sortilin

Ligandability

Cysteine 702 of Sortilin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

Cysteine 707 of Sortilin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

Cysteine 707 in protein B could not be asigned to a Uniprot residue.
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