ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Proline-, glutamic acid- and leucine-rich protein 1

Intermolecular
Cysteine 151 of WD repeat-containing protein 18 and cysteine 492
Cysteine 151 of WD repeat-containing protein 18 and cysteine 586
Intramolecular
Cysteine 287 and cysteine 371
Cysteine 572 and cysteine 625
Cysteine 252 and cysteine 260
Cysteine 287 and cysteine 289
Cysteine 492 and cysteine 586
Cysteine 670 and cysteine 677
Cysteine 252 and cysteine 289
Cysteine 289 and cysteine 371
A redox-regulated disulphide may form between cysteine 151 of WD repeat-containing protein 18 and cysteine 492 of Proline-, glutamic acid- and leucine-rich protein 1 (151 and 442 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
7uwf
Structure name
human rix1 sub-complex scaffold
Structure deposition date
2022-05-03
Thiol separation (Å)
8
Half-sphere exposure sum ?
75
Minimum pKa ?
12
% buried
98
Peptide A name
WD repeat-containing protein 18
Peptide B name
Proline-, glutamic acid- and leucine-rich protein 1
Peptide A accession
Q9BV38
Peptide B accession
C9JFV4
Peptide A residue number
151
Peptide B residue number
492

Ligandability

Cysteine 151 of WD repeat-containing protein 18

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 492 of Proline-, glutamic acid- and leucine-rich protein 1

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 between cysteine 151 of WD repeat-containing protein 18 and cysteine 586 of Proline-, glutamic acid- and leucine-rich protein 1 (151 and 536 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
7uwf
Structure name
human rix1 sub-complex scaffold
Structure deposition date
2022-05-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
78
Minimum pKa ?
12
% buried
98
Peptide A name
WD repeat-containing protein 18
Peptide B name
Proline-, glutamic acid- and leucine-rich protein 1
Peptide A accession
Q9BV38
Peptide B accession
C9JFV4
Peptide A residue number
151
Peptide B residue number
586

Ligandability

Cysteine 151 of WD repeat-containing protein 18

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 586 of Proline-, glutamic acid- and leucine-rich protein 1

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 Proline-, glutamic acid- and leucine-rich protein 1 between cysteines 287 and 371 (237 and 321 respectively in this structure).

Details

Redox score ?
70
PDB code
7uwf
Structure name
human rix1 sub-complex scaffold
Structure deposition date
2022-05-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
79
Minimum pKa ?
8
% buried
92
Peptide accession
C9JFV4
Residue number A
287
Residue number B
371
Peptide name
Proline-, glutamic acid- and leucine-rich protein 1

Ligandability

Cysteine 287 of Proline-, glutamic acid- and leucine-rich protein 1

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 371 of Proline-, glutamic acid- and leucine-rich protein 1

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 Proline-, glutamic acid- and leucine-rich protein 1 between cysteines 572 and 625 (522 and 575 respectively in this structure).

Details

Redox score ?
67
PDB code
7uwf
Structure name
human rix1 sub-complex scaffold
Structure deposition date
2022-05-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
86
Minimum pKa ?
7
% buried
94
Peptide accession
C9JFV4
Residue number A
572
Residue number B
625
Peptide name
Proline-, glutamic acid- and leucine-rich protein 1

Ligandability

Cysteine 572 of Proline-, glutamic acid- and leucine-rich protein 1

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 625 of Proline-, glutamic acid- and leucine-rich protein 1

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 Proline-, glutamic acid- and leucine-rich protein 1 between cysteines 252 and 260 (202 and 210 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
7uwf
Structure name
human rix1 sub-complex scaffold
Structure deposition date
2022-05-03
Thiol separation (Å)
5
Half-sphere exposure sum ?
82
Minimum pKa ?
12
% buried
90
Peptide accession
C9JFV4
Residue number A
252
Residue number B
260
Peptide name
Proline-, glutamic acid- and leucine-rich protein 1

Ligandability

Cysteine 252 of Proline-, glutamic acid- and leucine-rich protein 1

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 260 of Proline-, glutamic acid- and leucine-rich protein 1

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 Proline-, glutamic acid- and leucine-rich protein 1 between cysteines 287 and 289 (237 and 239 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
7uwf
Structure name
human rix1 sub-complex scaffold
Structure deposition date
2022-05-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
81
Minimum pKa ?
8
% buried
92
Peptide accession
C9JFV4
Residue number A
287
Residue number B
289
Peptide name
Proline-, glutamic acid- and leucine-rich protein 1

Ligandability

Cysteine 287 of Proline-, glutamic acid- and leucine-rich protein 1

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 289 of Proline-, glutamic acid- and leucine-rich protein 1

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 Proline-, glutamic acid- and leucine-rich protein 1 between cysteines 492 and 586 (442 and 536 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
28
PDB code
7uwf
Structure name
human rix1 sub-complex scaffold
Structure deposition date
2022-05-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
85
Minimum pKa ?
12
% buried
100
Peptide accession
C9JFV4
Residue number A
492
Residue number B
586
Peptide name
Proline-, glutamic acid- and leucine-rich protein 1

Ligandability

Cysteine 492 of Proline-, glutamic acid- and leucine-rich protein 1

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 586 of Proline-, glutamic acid- and leucine-rich protein 1

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 Proline-, glutamic acid- and leucine-rich protein 1 between cysteines 670 and 677 (620 and 627 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
26
PDB code
7uwf
Structure name
human rix1 sub-complex scaffold
Structure deposition date
2022-05-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
87
Minimum pKa ?
12
% buried
98
Peptide accession
C9JFV4
Residue number A
670
Residue number B
677
Peptide name
Proline-, glutamic acid- and leucine-rich protein 1

Ligandability

Cysteine 670 of Proline-, glutamic acid- and leucine-rich protein 1

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 677 of Proline-, glutamic acid- and leucine-rich protein 1

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 Proline-, glutamic acid- and leucine-rich protein 1 between cysteines 252 and 289 (202 and 239 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
24
PDB code
7uwf
Structure name
human rix1 sub-complex scaffold
Structure deposition date
2022-05-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
89
Minimum pKa ?
13
% buried
100
Peptide accession
C9JFV4
Residue number A
252
Residue number B
289
Peptide name
Proline-, glutamic acid- and leucine-rich protein 1

Ligandability

Cysteine 252 of Proline-, glutamic acid- and leucine-rich protein 1

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 289 of Proline-, glutamic acid- and leucine-rich protein 1

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 Proline-, glutamic acid- and leucine-rich protein 1 between cysteines 289 and 371 (239 and 321 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
23
PDB code
7uwf
Structure name
human rix1 sub-complex scaffold
Structure deposition date
2022-05-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
84
Minimum pKa ?
13
% buried
99
Peptide accession
C9JFV4
Residue number A
289
Residue number B
371
Peptide name
Proline-, glutamic acid- and leucine-rich protein 1

Ligandability

Cysteine 289 of Proline-, glutamic acid- and leucine-rich protein 1

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 371 of Proline-, glutamic acid- and leucine-rich protein 1

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.

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