ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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THO complex subunit 6 homolog

Intramolecular
Cysteine 35 and cysteine 314 L
Cysteine 214 and cysteine 235
Cysteine 173 and cysteine 225
Cysteine 225 and cysteine 235
Cysteine 173 and cysteine 235
A redox-regulated disulphide may form within THO complex subunit 6 homolog between cysteines 35 and 314. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
7apk
Structure name
structure of the human tho - uap56 complex
Structure deposition date
2020-10-17
Thiol separation (Å)
8
Half-sphere exposure sum ?
62
Minimum pKa ?
8
% buried
24
Peptide accession
Q86W42
Residue number A
35
Residue number B
314
Peptide name
THO complex subunit 6 homolog

Ligandability

Cysteine 35 of THO complex subunit 6 homolog

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

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.

Cysteine 314 of THO complex subunit 6 homolog

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 THO complex subunit 6 homolog between cysteines 214 and 235. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
7apk
Structure name
structure of the human tho - uap56 complex
Structure deposition date
2020-10-17
Thiol separation (Å)
8
Half-sphere exposure sum ?
89
Minimum pKa ?
11
% buried
74
Peptide accession
Q86W42
Residue number A
214
Residue number B
235
Peptide name
THO complex subunit 6 homolog

Ligandability

Cysteine 214 of THO complex subunit 6 homolog

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 235 of THO complex subunit 6 homolog

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 THO complex subunit 6 homolog between cysteines 173 and 225. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
7apk
Structure name
structure of the human tho - uap56 complex
Structure deposition date
2020-10-17
Thiol separation (Å)
6
Half-sphere exposure sum ?
92
Minimum pKa ?
12
% buried
100
Peptide accession
Q86W42
Residue number A
173
Residue number B
225
Peptide name
THO complex subunit 6 homolog

Ligandability

Cysteine 173 of THO complex subunit 6 homolog

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 225 of THO complex subunit 6 homolog

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 THO complex subunit 6 homolog between cysteines 225 and 235. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
7apk
Structure name
structure of the human tho - uap56 complex
Structure deposition date
2020-10-17
Thiol separation (Å)
7
Half-sphere exposure sum ?
102
Minimum pKa ?
12
% buried
100
Peptide accession
Q86W42
Residue number A
225
Residue number B
235
Peptide name
THO complex subunit 6 homolog

Ligandability

Cysteine 225 of THO complex subunit 6 homolog

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 235 of THO complex subunit 6 homolog

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 THO complex subunit 6 homolog between cysteines 173 and 235. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
7apk
Structure name
structure of the human tho - uap56 complex
Structure deposition date
2020-10-17
Thiol separation (Å)
7
Half-sphere exposure sum ?
100
Minimum pKa ?
13
% buried
100
Peptide accession
Q86W42
Residue number A
173
Residue number B
235
Peptide name
THO complex subunit 6 homolog

Ligandability

Cysteine 173 of THO complex subunit 6 homolog

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 235 of THO complex subunit 6 homolog

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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