ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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StAR-related lipid transfer protein 4

Intramolecular
Cysteine 96 and cysteine 97
Cysteine 96 and cysteine 132
Cysteine 132 and cysteine 153
A redox-regulated disulphide may form within StAR-related lipid transfer protein 4 between cysteines 96 and 97. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
6l1d
Structure name
structure of human star-related lipid transfer protein 4
Structure deposition date
2019-09-29
Thiol separation (Å)
8
Half-sphere exposure sum ?
64
Minimum pKa ?
11
% buried
43
Peptide accession
Q96DR4
Residue number A
96
Residue number B
97
Peptide name
StAR-related lipid transfer protein 4

Ligandability

Cysteine 96 of StAR-related lipid transfer protein 4

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 97 of StAR-related lipid transfer protein 4

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 4 between cysteines 96 and 132. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
6l1m
Structure name
structure of human star-related lipid transfer protein 4 mutant - lwni107-110gg
Structure deposition date
2019-09-29
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
11
% buried
62
Peptide accession
Q96DR4
Residue number A
96
Residue number B
132
Peptide name
StAR-related lipid transfer protein 4

Ligandability

Cysteine 96 of StAR-related lipid transfer protein 4

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 132 of StAR-related lipid transfer protein 4

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 4 between cysteines 132 and 153. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
6l1d
Structure name
structure of human star-related lipid transfer protein 4
Structure deposition date
2019-09-29
Thiol separation (Å)
8
Half-sphere exposure sum ?
87
Minimum pKa ?
12
% buried
94
Peptide accession
Q96DR4
Residue number A
132
Residue number B
153
Peptide name
StAR-related lipid transfer protein 4

Ligandability

Cysteine 132 of StAR-related lipid transfer protein 4

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 153 of StAR-related lipid transfer protein 4

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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