ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Teneurin-2

Intramolecular
Cysteine 1403 and cysteine 1456
Cysteine 1522 and cysteine 1530
Cysteine 1336 and cysteine 1344
Cysteine 1520 and cysteine 1528
Cysteine 1511 and cysteine 1771
Cysteine 1528 and cysteine 1530
Cysteine 1520 and cysteine 1530
Cysteine 1522 and cysteine 1528
Cysteine 1520 and cysteine 1522
A redox-regulated disulphide may form within Teneurin-2 between cysteines 1403 and 1456 (1277 and 1330 respectively in this structure).

Details

Redox score ?
88
PDB code
6vhh
Structure name
human teneurin-2 and human latrophilin-3 binary complex
Structure deposition date
2020-01-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
38
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NT68
Residue number A
1403
Residue number B
1456
Peptide name
Teneurin-2

Ligandability

Cysteine 1403 of Teneurin-2

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 1456 of Teneurin-2

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 Teneurin-2 between cysteines 1522 and 1530 (1396 and 1404 respectively in this structure).

Details

Redox score ?
86
PDB code
6vhh
Structure name
human teneurin-2 and human latrophilin-3 binary complex
Structure deposition date
2020-01-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NT68
Residue number A
1522
Residue number B
1530
Peptide name
Teneurin-2

Ligandability

Cysteine 1522 of Teneurin-2

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 1530 of Teneurin-2

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 Teneurin-2 between cysteines 1336 and 1344 (1210 and 1218 respectively in this structure).

Details

Redox score ?
86
PDB code
6vhh
Structure name
human teneurin-2 and human latrophilin-3 binary complex
Structure deposition date
2020-01-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NT68
Residue number A
1336
Residue number B
1344
Peptide name
Teneurin-2

Ligandability

Cysteine 1336 of Teneurin-2

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 1344 of Teneurin-2

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 Teneurin-2 between cysteines 1520 and 1528 (1394 and 1402 respectively in this structure).

Details

Redox score ?
85
PDB code
6vhh
Structure name
human teneurin-2 and human latrophilin-3 binary complex
Structure deposition date
2020-01-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
37
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NT68
Residue number A
1520
Residue number B
1528
Peptide name
Teneurin-2

Ligandability

Cysteine 1520 of Teneurin-2

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 1528 of Teneurin-2

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 Teneurin-2 between cysteines 1511 and 1771 (1385 and 1645 respectively in this structure).

Details

Redox score ?
77
PDB code
6vhh
Structure name
human teneurin-2 and human latrophilin-3 binary complex
Structure deposition date
2020-01-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
5
% buried
56
Peptide accession
Q9NT68
Residue number A
1511
Residue number B
1771
Peptide name
Teneurin-2

Ligandability

Cysteine 1511 of Teneurin-2

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 1771 of Teneurin-2

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 Teneurin-2 between cysteines 1528 and 1530 (1402 and 1404 respectively in this structure).

Details

Redox score ?
70
PDB code
6vhh
Structure name
human teneurin-2 and human latrophilin-3 binary complex
Structure deposition date
2020-01-09
Thiol separation (Å)
5
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NT68
Residue number A
1528
Residue number B
1530
Peptide name
Teneurin-2

Ligandability

Cysteine 1528 of Teneurin-2

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 1530 of Teneurin-2

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 Teneurin-2 between cysteines 1520 and 1530 (1394 and 1404 respectively in this structure).

Details

Redox score ?
64
PDB code
6vhh
Structure name
human teneurin-2 and human latrophilin-3 binary complex
Structure deposition date
2020-01-09
Thiol separation (Å)
6
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NT68
Residue number A
1520
Residue number B
1530
Peptide name
Teneurin-2

Ligandability

Cysteine 1520 of Teneurin-2

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 1530 of Teneurin-2

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 Teneurin-2 between cysteines 1522 and 1528 (1396 and 1402 respectively in this structure).

Details

Redox score ?
62
PDB code
6vhh
Structure name
human teneurin-2 and human latrophilin-3 binary complex
Structure deposition date
2020-01-09
Thiol separation (Å)
6
Half-sphere exposure sum ?
41
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NT68
Residue number A
1522
Residue number B
1528
Peptide name
Teneurin-2

Ligandability

Cysteine 1522 of Teneurin-2

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 1528 of Teneurin-2

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 Teneurin-2 between cysteines 1520 and 1522 (1394 and 1396 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
6vhh
Structure name
human teneurin-2 and human latrophilin-3 binary complex
Structure deposition date
2020-01-09
Thiol separation (Å)
7
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NT68
Residue number A
1520
Residue number B
1522
Peptide name
Teneurin-2

Ligandability

Cysteine 1520 of Teneurin-2

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 1522 of Teneurin-2

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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