ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Transforming growth factor beta regulator 1

Intramolecular
Cysteine 227 and cysteine 232
Cysteine 236 and cysteine 267
Cysteine 217 and cysteine 236
A redox-regulated disulphide may form within Transforming growth factor beta regulator 1 between cysteines 227 and 232. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
2wzo
Structure name
the structure of the fyr domain
Structure deposition date
2009-12-01
Thiol separation (Å)
9
Half-sphere exposure sum ?
42
Minimum pKa ?
10
% buried
14
Peptide accession
Q3YBR2
Residue number A
227
Residue number B
232
Peptide name
Transforming growth factor beta regulator 1

Ligandability

Cysteine 227 of Transforming growth factor beta regulator 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.

Cysteine 232 of Transforming growth factor beta regulator 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 Transforming growth factor beta regulator 1 between cysteines 236 and 267. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
2wzo
Structure name
the structure of the fyr domain
Structure deposition date
2009-12-01
Thiol separation (Å)
8
Half-sphere exposure sum ?
80
Minimum pKa ?
11
% buried
80
Peptide accession
Q3YBR2
Residue number A
236
Residue number B
267
Peptide name
Transforming growth factor beta regulator 1

Ligandability

Cysteine 236 of Transforming growth factor beta regulator 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.

Cysteine 267 of Transforming growth factor beta regulator 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 Transforming growth factor beta regulator 1 between cysteines 217 and 236. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
2wzo
Structure name
the structure of the fyr domain
Structure deposition date
2009-12-01
Thiol separation (Å)
8
Half-sphere exposure sum ?
79
Minimum pKa ?
10
% buried
70
Peptide accession
Q3YBR2
Residue number A
217
Residue number B
236
Peptide name
Transforming growth factor beta regulator 1

Ligandability

Cysteine 217 of Transforming growth factor beta regulator 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.

Cysteine 236 of Transforming growth factor beta regulator 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.

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