ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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StAR-related lipid transfer protein 5

Intramolecular
Cysteine 158 and cysteine 160
Cysteine 67 and cysteine 160
Cysteine 156 and cysteine 158
A redox-regulated disulphide may form within StAR-related lipid transfer protein 5 between cysteines 158 and 160. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
2r55
Structure name
human star-related lipid transfer protein 5
Structure deposition date
2007-09-03
Thiol separation (Å)
6
Half-sphere exposure sum ?
84
Minimum pKa ?
11
% buried
96
Peptide accession
Q9NSY2
Residue number A
158
Residue number B
160
Peptide name
StAR-related lipid transfer protein 5

Ligandability

Cysteine 158 of StAR-related lipid transfer protein 5

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 160 of StAR-related lipid transfer protein 5

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 StAR-related lipid transfer protein 5 between cysteines 67 and 160. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
2r55
Structure name
human star-related lipid transfer protein 5
Structure deposition date
2007-09-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
12
% buried
81
Peptide accession
Q9NSY2
Residue number A
67
Residue number B
160
Peptide name
StAR-related lipid transfer protein 5

Ligandability

Cysteine 67 of StAR-related lipid transfer protein 5

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 160 of StAR-related lipid transfer protein 5

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 StAR-related lipid transfer protein 5 between cysteines 156 and 158. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
2r55
Structure name
human star-related lipid transfer protein 5
Structure deposition date
2007-09-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
86
Minimum pKa ?
11
% buried
100
Peptide accession
Q9NSY2
Residue number A
156
Residue number B
158
Peptide name
StAR-related lipid transfer protein 5

Ligandability

Cysteine 156 of StAR-related lipid transfer protein 5

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 158 of StAR-related lipid transfer protein 5

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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