ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Transformation/transcription domain-associated protein

Intermolecular
Cysteine 2657 and cysteine 263 of Transcriptional adapter 1
Intramolecular
Cysteine 1868 and cysteine 1874 L
Cysteine 1874 and cysteine 1879 L
Cysteine 1868 and cysteine 1879 L
Cysteine 3555 and cysteine 3758
Cysteine 1146 and cysteine 1149
Cysteine 1148 and cysteine 1149
Cysteine 2200 and cysteine 2203
Cysteine 1099 and cysteine 1108
Cysteine 1146 and cysteine 1148
More...
Cysteine 2657 and cysteine 2691 L
Cysteine 1099 and cysteine 1148
Cysteine 2495 and cysteine 2674
A redox-regulated disulphide may form between cysteine 2657 of Transformation/transcription domain-associated protein and cysteine 263 of Transcriptional adapter 1.

Details

Redox score ?
72
PDB code
8h7g
Structure name
cryo-em structure of the human saga complex
Structure deposition date
2022-10-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
77
Minimum pKa ?
7
% buried
70
Peptide A name
Transformation/transcription domain-associated protein
Peptide B name
Transcriptional adapter 1
Peptide A accession
Q9Y4A5
Peptide B accession
Q96BN2
Peptide A residue number
2657
Peptide B residue number
263

Ligandability

Cysteine 2657 of Transformation/transcription domain-associated protein

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 263 of Transcriptional adapter 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 Transformation/transcription domain-associated protein between cysteines 1868 and 1874.

Details

Redox score ?
87
PDB code
8h7g
Structure name
cryo-em structure of the human saga complex
Structure deposition date
2022-10-20
Thiol separation (Å)
2
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9Y4A5
Residue number A
1868
Residue number B
1874
Peptide name
Transformation/transcription domain-associated protein

Ligandability

Cysteine 1868 of Transformation/transcription domain-associated protein

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 1874 of Transformation/transcription domain-associated protein

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 Transformation/transcription domain-associated protein between cysteines 1874 and 1879.

Details

Redox score ?
73
PDB code
8h7g
Structure name
cryo-em structure of the human saga complex
Structure deposition date
2022-10-20
Thiol separation (Å)
3
Half-sphere exposure sum ?
62
Minimum pKa ?
11
% buried
nan
Peptide accession
Q9Y4A5
Residue number A
1874
Residue number B
1879
Peptide name
Transformation/transcription domain-associated protein

Ligandability

Cysteine 1874 of Transformation/transcription domain-associated protein

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 1879 of Transformation/transcription domain-associated protein

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 Transformation/transcription domain-associated protein between cysteines 1868 and 1879.

Details

Redox score ?
68
PDB code
8h7g
Structure name
cryo-em structure of the human saga complex
Structure deposition date
2022-10-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
11
% buried
nan
Peptide accession
Q9Y4A5
Residue number A
1868
Residue number B
1879
Peptide name
Transformation/transcription domain-associated protein

Ligandability

Cysteine 1868 of Transformation/transcription domain-associated protein

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 1879 of Transformation/transcription domain-associated protein

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 Transformation/transcription domain-associated protein between cysteines 3555 and 3758. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
8h7g
Structure name
cryo-em structure of the human saga complex
Structure deposition date
2022-10-20
Thiol separation (Å)
7
Half-sphere exposure sum ?
66
Minimum pKa ?
10
% buried
74
Peptide accession
Q9Y4A5
Residue number A
3555
Residue number B
3758
Peptide name
Transformation/transcription domain-associated protein

Ligandability

Cysteine 3555 of Transformation/transcription domain-associated protein

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 3758 of Transformation/transcription domain-associated protein

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 Transformation/transcription domain-associated protein between cysteines 1146 and 1149. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
8h7g
Structure name
cryo-em structure of the human saga complex
Structure deposition date
2022-10-20
Thiol separation (Å)
6
Half-sphere exposure sum ?
81
Minimum pKa ?
11
% buried
93
Peptide accession
Q9Y4A5
Residue number A
1146
Residue number B
1149
Peptide name
Transformation/transcription domain-associated protein

Ligandability

Cysteine 1146 of Transformation/transcription domain-associated protein

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 1149 of Transformation/transcription domain-associated protein

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 Transformation/transcription domain-associated protein between cysteines 1148 and 1149. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
8h7g
Structure name
cryo-em structure of the human saga complex
Structure deposition date
2022-10-20
Thiol separation (Å)
7
Half-sphere exposure sum ?
77
Minimum pKa ?
11
% buried
92
Peptide accession
Q9Y4A5
Residue number A
1148
Residue number B
1149
Peptide name
Transformation/transcription domain-associated protein

Ligandability

Cysteine 1148 of Transformation/transcription domain-associated protein

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 1149 of Transformation/transcription domain-associated protein

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 Transformation/transcription domain-associated protein between cysteines 2200 and 2203. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
8h7g
Structure name
cryo-em structure of the human saga complex
Structure deposition date
2022-10-20
Thiol separation (Å)
9
Half-sphere exposure sum ?
48
Minimum pKa ?
9
% buried
14
Peptide accession
Q9Y4A5
Residue number A
2200
Residue number B
2203
Peptide name
Transformation/transcription domain-associated protein

Ligandability

Cysteine 2200 of Transformation/transcription domain-associated protein

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 2203 of Transformation/transcription domain-associated protein

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 Transformation/transcription domain-associated protein between cysteines 1099 and 1108. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
8h7g
Structure name
cryo-em structure of the human saga complex
Structure deposition date
2022-10-20
Thiol separation (Å)
8
Half-sphere exposure sum ?
73
Minimum pKa ?
10
% buried
72
Peptide accession
Q9Y4A5
Residue number A
1099
Residue number B
1108
Peptide name
Transformation/transcription domain-associated protein

Ligandability

Cysteine 1099 of Transformation/transcription domain-associated protein

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 1108 of Transformation/transcription domain-associated protein

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 Transformation/transcription domain-associated protein between cysteines 1146 and 1148. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
8h7g
Structure name
cryo-em structure of the human saga complex
Structure deposition date
2022-10-20
Thiol separation (Å)
9
Half-sphere exposure sum ?
74
Minimum pKa ?
12
% buried
90
Peptide accession
Q9Y4A5
Residue number A
1146
Residue number B
1148
Peptide name
Transformation/transcription domain-associated protein

Ligandability

Cysteine 1146 of Transformation/transcription domain-associated protein

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 1148 of Transformation/transcription domain-associated protein

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 Transformation/transcription domain-associated protein between cysteines 2657 and 2691. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
8h7g
Structure name
cryo-em structure of the human saga complex
Structure deposition date
2022-10-20
Thiol separation (Å)
10
Half-sphere exposure sum ?
73
Minimum pKa ?
11
% buried
68
Peptide accession
Q9Y4A5
Residue number A
2657
Residue number B
2691
Peptide name
Transformation/transcription domain-associated protein

Ligandability

Cysteine 2657 of Transformation/transcription domain-associated protein

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 2691 of Transformation/transcription domain-associated protein

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.

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 Transformation/transcription domain-associated protein between cysteines 1099 and 1148. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
8h7g
Structure name
cryo-em structure of the human saga complex
Structure deposition date
2022-10-20
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
12
% buried
90
Peptide accession
Q9Y4A5
Residue number A
1099
Residue number B
1148
Peptide name
Transformation/transcription domain-associated protein

Ligandability

Cysteine 1099 of Transformation/transcription domain-associated protein

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 1148 of Transformation/transcription domain-associated protein

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 Transformation/transcription domain-associated protein between cysteines 2495 and 2674. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
28
PDB code
8h7g
Structure name
cryo-em structure of the human saga complex
Structure deposition date
2022-10-20
Thiol separation (Å)
10
Half-sphere exposure sum ?
65
Minimum pKa ?
12
% buried
90
Peptide accession
Q9Y4A5
Residue number A
2495
Residue number B
2674
Peptide name
Transformation/transcription domain-associated protein

Ligandability

Cysteine 2495 of Transformation/transcription domain-associated protein

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 2674 of Transformation/transcription domain-associated protein

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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