ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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SHC-transforming protein 1

Intramolecular
Cysteine 196 and cysteine 212
Cysteine 169 and cysteine 287
Cysteine 196 and cysteine 287
A redox-regulated disulphide may form within SHC-transforming protein 1 between cysteines 196 and 212 (86 and 102 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
1n3h
Structure name
coupling of folding and binding in the ptb domain of the signaling protein shc
Structure deposition date
2002-10-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
60
Minimum pKa ?
10
% buried
32
Peptide accession
P29353
Residue number A
196
Residue number B
212
Peptide name
SHC-transforming protein 1

Ligandability

Cysteine 196 of SHC-transforming protein 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 212 of SHC-transforming protein 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 SHC-transforming protein 1 between cysteines 169 and 287 (59 and 177 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
1shc
Structure name
shc ptb domain complexed with a trka receptor phosphopeptide, nmr, minimized average structure
Structure deposition date
1996-03-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
74
Minimum pKa ?
10
% buried
76
Peptide accession
P29353
Residue number A
169
Residue number B
287
Peptide name
SHC-transforming protein 1

Ligandability

Cysteine 169 of SHC-transforming protein 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 287 of SHC-transforming protein 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 SHC-transforming protein 1 between cysteines 196 and 287 (86 and 177 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
29
PDB code
1shc
Structure name
shc ptb domain complexed with a trka receptor phosphopeptide, nmr, minimized average structure
Structure deposition date
1996-03-27
Thiol separation (Å)
10
Half-sphere exposure sum ?
74
Minimum pKa ?
11
% buried
76
Peptide accession
P29353
Residue number A
196
Residue number B
287
Peptide name
SHC-transforming protein 1

Ligandability

Cysteine 196 of SHC-transforming protein 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 287 of SHC-transforming protein 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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