ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Teneurin-4

Intermolecular
Cysteine 2466 and cysteine 2466
Intramolecular
Cysteine 1395 and cysteine 1448
Cysteine 1217 and cysteine 1220
Cysteine 1011 and cysteine 1145
Cysteine 838 and cysteine 857
Cysteine 1328 and cysteine 1336
Cysteine 1513 and cysteine 1521
Cysteine 858 and cysteine 869
Cysteine 1515 and cysteine 1523
Cysteine 852 and cysteine 863
More...
Cysteine 1035 and cysteine 2524
Cysteine 1237 and cysteine 1545
Cysteine 863 and cysteine 869
Cysteine 857 and cysteine 863
Cysteine 838 and cysteine 863
Cysteine 852 and cysteine 869
Cysteine 1521 and cysteine 1523
Cysteine 1515 and cysteine 1521
Cysteine 858 and cysteine 863
Cysteine 852 and cysteine 857
Cysteine 838 and cysteine 852
Cysteine 857 and cysteine 869
Cysteine 852 and cysteine 858
Cysteine 1513 and cysteine 1523
Cysteine 857 and cysteine 858
Cysteine 1513 and cysteine 1515
Cysteine 838 and cysteine 869
Cysteine 838 and cysteine 858
A redox-regulated disulphide may form between two units of Teneurin-4 at cysteines 2466 and 2466 (2585 and 2585 respectively in this structure).

Details

Redox score ?
84
PDB code
7ban
Structure name
human teneurin4 mut c2
Structure deposition date
2020-12-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
42
Minimum pKa ?
nan
% buried
nan
Peptide A name
Teneurin-4
Peptide B name
Teneurin-4
Peptide A accession
Q6N022
Peptide B accession
Q6N022
Peptide A residue number
2466
Peptide B residue number
2466

Ligandability

A redox-regulated disulphide may form within Teneurin-4 between cysteines 1395 and 1448.

Details

Redox score ?
91
PDB code
7bam
Structure name
human teneurin4 wt c2
Structure deposition date
2020-12-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6N022
Residue number A
1395
Residue number B
1448
Peptide name
Teneurin-4

Ligandability

Cysteine 1395 of Teneurin-4

Cysteine 1448 of Teneurin-4

A redox-regulated disulphide may form within Teneurin-4 between cysteines 1217 and 1220.

Details

Redox score ?
89
PDB code
7bam
Structure name
human teneurin4 wt c2
Structure deposition date
2020-12-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6N022
Residue number A
1217
Residue number B
1220
Peptide name
Teneurin-4

Ligandability

Cysteine 1217 of Teneurin-4

Cysteine 1220 of Teneurin-4

A redox-regulated disulphide may form within Teneurin-4 between cysteines 1011 and 1145.

Details

Redox score ?
88
PDB code
7bam
Structure name
human teneurin4 wt c2
Structure deposition date
2020-12-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
38
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6N022
Residue number A
1011
Residue number B
1145
Peptide name
Teneurin-4

Ligandability

Cysteine 1011 of Teneurin-4

Cysteine 1145 of Teneurin-4

A redox-regulated disulphide may form within Teneurin-4 between cysteines 838 and 857 (13 and 32 respectively in this structure).

Details

Redox score ?
87
PDB code
7plp
Structure name
human teneurin-4 c-rich domain
Structure deposition date
2021-09-01
Thiol separation (Å)
2
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6N022
Residue number A
838
Residue number B
857
Peptide name
Teneurin-4

Ligandability

Cysteine 838 of Teneurin-4

Cysteine 857 of Teneurin-4

A redox-regulated disulphide may form within Teneurin-4 between cysteines 1328 and 1336.

Details

Redox score ?
87
PDB code
7bao
Structure name
human teneurin4 mut c1
Structure deposition date
2020-12-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
45
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6N022
Residue number A
1328
Residue number B
1336
Peptide name
Teneurin-4

Ligandability

Cysteine 1328 of Teneurin-4

Cysteine 1336 of Teneurin-4

A redox-regulated disulphide may form within Teneurin-4 between cysteines 1513 and 1521.

Details

Redox score ?
87
PDB code
7bao
Structure name
human teneurin4 mut c1
Structure deposition date
2020-12-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
36
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6N022
Residue number A
1513
Residue number B
1521
Peptide name
Teneurin-4

Ligandability

Cysteine 1513 of Teneurin-4

Cysteine 1521 of Teneurin-4

A redox-regulated disulphide may form within Teneurin-4 between cysteines 858 and 869 (33 and 44 respectively in this structure).

Details

Redox score ?
86
PDB code
7plp
Structure name
human teneurin-4 c-rich domain
Structure deposition date
2021-09-01
Thiol separation (Å)
2
Half-sphere exposure sum ?
47
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6N022
Residue number A
858
Residue number B
869
Peptide name
Teneurin-4

Ligandability

Cysteine 858 of Teneurin-4

Cysteine 869 of Teneurin-4

A redox-regulated disulphide may form within Teneurin-4 between cysteines 1515 and 1523.

Details

Redox score ?
86
PDB code
7ban
Structure name
human teneurin4 mut c2
Structure deposition date
2020-12-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6N022
Residue number A
1515
Residue number B
1523
Peptide name
Teneurin-4

Ligandability

Cysteine 1515 of Teneurin-4

Cysteine 1523 of Teneurin-4

A redox-regulated disulphide may form within Teneurin-4 between cysteines 852 and 863 (27 and 38 respectively in this structure).

Details

Redox score ?
85
PDB code
7plp
Structure name
human teneurin-4 c-rich domain
Structure deposition date
2021-09-01
Thiol separation (Å)
2
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6N022
Residue number A
852
Residue number B
863
Peptide name
Teneurin-4

Ligandability

Cysteine 852 of Teneurin-4

Cysteine 863 of Teneurin-4

A redox-regulated disulphide may form within Teneurin-4 between cysteines 1035 and 2524.

Details

Redox score ?
85
PDB code
7bam
Structure name
human teneurin4 wt c2
Structure deposition date
2020-12-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6N022
Residue number A
1035
Residue number B
2524
Peptide name
Teneurin-4

Ligandability

Cysteine 1035 of Teneurin-4

Cysteine 2524 of Teneurin-4

A redox-regulated disulphide may form within Teneurin-4 between cysteines 1237 and 1545.

Details

Redox score ?
79
PDB code
7bao
Structure name
human teneurin4 mut c1
Structure deposition date
2020-12-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6N022
Residue number A
1237
Residue number B
1545
Peptide name
Teneurin-4

Ligandability

Cysteine 1237 of Teneurin-4

Cysteine 1545 of Teneurin-4

A redox-regulated disulphide may form within Teneurin-4 between cysteines 863 and 869 (38 and 44 respectively in this structure).

Details

Redox score ?
72
PDB code
7plp
Structure name
human teneurin-4 c-rich domain
Structure deposition date
2021-09-01
Thiol separation (Å)
5
Half-sphere exposure sum ?
45
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6N022
Residue number A
863
Residue number B
869
Peptide name
Teneurin-4

Ligandability

Cysteine 863 of Teneurin-4

Cysteine 869 of Teneurin-4

A redox-regulated disulphide may form within Teneurin-4 between cysteines 857 and 863 (32 and 38 respectively in this structure).

Details

Redox score ?
71
PDB code
7plp
Structure name
human teneurin-4 c-rich domain
Structure deposition date
2021-09-01
Thiol separation (Å)
5
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6N022
Residue number A
857
Residue number B
863
Peptide name
Teneurin-4

Ligandability

Cysteine 857 of Teneurin-4

Cysteine 863 of Teneurin-4

A redox-regulated disulphide may form within Teneurin-4 between cysteines 838 and 863 (13 and 38 respectively in this structure).

Details

Redox score ?
67
PDB code
7plp
Structure name
human teneurin-4 c-rich domain
Structure deposition date
2021-09-01
Thiol separation (Å)
5
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6N022
Residue number A
838
Residue number B
863
Peptide name
Teneurin-4

Ligandability

Cysteine 838 of Teneurin-4

Cysteine 863 of Teneurin-4

A redox-regulated disulphide may form within Teneurin-4 between cysteines 852 and 869 (27 and 44 respectively in this structure).

Details

Redox score ?
66
PDB code
7plp
Structure name
human teneurin-4 c-rich domain
Structure deposition date
2021-09-01
Thiol separation (Å)
5
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6N022
Residue number A
852
Residue number B
869
Peptide name
Teneurin-4

Ligandability

Cysteine 852 of Teneurin-4

Cysteine 869 of Teneurin-4

A redox-regulated disulphide may form within Teneurin-4 between cysteines 1521 and 1523.

Details

Redox score ?
63
PDB code
7ban
Structure name
human teneurin4 mut c2
Structure deposition date
2020-12-16
Thiol separation (Å)
6
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6N022
Residue number A
1521
Residue number B
1523
Peptide name
Teneurin-4

Ligandability

Cysteine 1521 of Teneurin-4

Cysteine 1523 of Teneurin-4

A redox-regulated disulphide may form within Teneurin-4 between cysteines 1515 and 1521.

Details

Redox score ?
63
PDB code
7bam
Structure name
human teneurin4 wt c2
Structure deposition date
2020-12-16
Thiol separation (Å)
6
Half-sphere exposure sum ?
43
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6N022
Residue number A
1515
Residue number B
1521
Peptide name
Teneurin-4

Ligandability

Cysteine 1515 of Teneurin-4

Cysteine 1521 of Teneurin-4

A redox-regulated disulphide may form within Teneurin-4 between cysteines 858 and 863 (33 and 38 respectively in this structure).

Details

Redox score ?
62
PDB code
7plp
Structure name
human teneurin-4 c-rich domain
Structure deposition date
2021-09-01
Thiol separation (Å)
6
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6N022
Residue number A
858
Residue number B
863
Peptide name
Teneurin-4

Ligandability

Cysteine 858 of Teneurin-4

Cysteine 863 of Teneurin-4

A redox-regulated disulphide may form within Teneurin-4 between cysteines 852 and 857 (27 and 32 respectively in this structure).

Details

Redox score ?
61
PDB code
7plp
Structure name
human teneurin-4 c-rich domain
Structure deposition date
2021-09-01
Thiol separation (Å)
6
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6N022
Residue number A
852
Residue number B
857
Peptide name
Teneurin-4

Ligandability

Cysteine 852 of Teneurin-4

Cysteine 857 of Teneurin-4

A redox-regulated disulphide may form within Teneurin-4 between cysteines 838 and 852 (13 and 27 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
7plp
Structure name
human teneurin-4 c-rich domain
Structure deposition date
2021-09-01
Thiol separation (Å)
7
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6N022
Residue number A
838
Residue number B
852
Peptide name
Teneurin-4

Ligandability

Cysteine 838 of Teneurin-4

Cysteine 852 of Teneurin-4

A redox-regulated disulphide may form within Teneurin-4 between cysteines 857 and 869 (32 and 44 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
7plp
Structure name
human teneurin-4 c-rich domain
Structure deposition date
2021-09-01
Thiol separation (Å)
8
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6N022
Residue number A
857
Residue number B
869
Peptide name
Teneurin-4

Ligandability

Cysteine 857 of Teneurin-4

Cysteine 869 of Teneurin-4

A redox-regulated disulphide may form within Teneurin-4 between cysteines 852 and 858 (27 and 33 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
7plp
Structure name
human teneurin-4 c-rich domain
Structure deposition date
2021-09-01
Thiol separation (Å)
7
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6N022
Residue number A
852
Residue number B
858
Peptide name
Teneurin-4

Ligandability

Cysteine 852 of Teneurin-4

Cysteine 858 of Teneurin-4

A redox-regulated disulphide may form within Teneurin-4 between cysteines 1513 and 1523. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
7ban
Structure name
human teneurin4 mut c2
Structure deposition date
2020-12-16
Thiol separation (Å)
8
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6N022
Residue number A
1513
Residue number B
1523
Peptide name
Teneurin-4

Ligandability

Cysteine 1513 of Teneurin-4

Cysteine 1523 of Teneurin-4

A redox-regulated disulphide may form within Teneurin-4 between cysteines 857 and 858 (32 and 33 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
7plp
Structure name
human teneurin-4 c-rich domain
Structure deposition date
2021-09-01
Thiol separation (Å)
7
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6N022
Residue number A
857
Residue number B
858
Peptide name
Teneurin-4

Ligandability

Cysteine 857 of Teneurin-4

Cysteine 858 of Teneurin-4

A redox-regulated disulphide may form within Teneurin-4 between cysteines 1513 and 1515. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
7bam
Structure name
human teneurin4 wt c2
Structure deposition date
2020-12-16
Thiol separation (Å)
7
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6N022
Residue number A
1513
Residue number B
1515
Peptide name
Teneurin-4

Ligandability

Cysteine 1513 of Teneurin-4

Cysteine 1515 of Teneurin-4

A redox-regulated disulphide may form within Teneurin-4 between cysteines 838 and 869 (13 and 44 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
7plp
Structure name
human teneurin-4 c-rich domain
Structure deposition date
2021-09-01
Thiol separation (Å)
9
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6N022
Residue number A
838
Residue number B
869
Peptide name
Teneurin-4

Ligandability

Cysteine 838 of Teneurin-4

Cysteine 869 of Teneurin-4

A redox-regulated disulphide may form within Teneurin-4 between cysteines 838 and 858 (13 and 33 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
7plp
Structure name
human teneurin-4 c-rich domain
Structure deposition date
2021-09-01
Thiol separation (Å)
8
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6N022
Residue number A
838
Residue number B
858
Peptide name
Teneurin-4

Ligandability

Cysteine 838 of Teneurin-4

Cysteine 858 of Teneurin-4

If this tool was useful for finding a disulphide, please cite: