ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Tetratricopeptide repeat domain 8

Intramolecular
Cysteine 19 and cysteine 23
Cysteine 355 and cysteine 356
Cysteine 282 and cysteine 317
A redox-regulated disulphide may form within Tetratricopeptide repeat domain 8 between cysteines 19 and 23. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
6vbv
Structure name
structure of the bovine bbsome:arl6:gtp complex
Structure deposition date
2019-12-19
Thiol separation (Å)
6
Half-sphere exposure sum ?
73
Minimum pKa ?
11
% buried
67
Peptide accession
F1N4X0
Residue number A
19
Residue number B
23
Peptide name
Tetratricopeptide repeat domain 8

Ligandability

Cysteine 19 of Tetratricopeptide repeat domain 8

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 23 of Tetratricopeptide repeat domain 8

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 Tetratricopeptide repeat domain 8 between cysteines 355 and 356. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
6voa
Structure name
cryo-em structure of the bbsome-arl6 complex
Structure deposition date
2020-01-30
Thiol separation (Å)
7
Half-sphere exposure sum ?
80
Minimum pKa ?
11
% buried
100
Peptide accession
F1N4X0
Residue number A
355
Residue number B
356
Peptide name
Tetratricopeptide repeat domain 8

Ligandability

Cysteine 355 of Tetratricopeptide repeat domain 8

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 356 of Tetratricopeptide repeat domain 8

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 Tetratricopeptide repeat domain 8 between cysteines 282 and 317. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
6vbv
Structure name
structure of the bovine bbsome:arl6:gtp complex
Structure deposition date
2019-12-19
Thiol separation (Å)
7
Half-sphere exposure sum ?
79
Minimum pKa ?
14
% buried
100
Peptide accession
F1N4X0
Residue number A
282
Residue number B
317
Peptide name
Tetratricopeptide repeat domain 8

Ligandability

Cysteine 282 of Tetratricopeptide repeat domain 8

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 317 of Tetratricopeptide repeat domain 8

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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