ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Oxysterol-binding protein 1

Intramolecular
Cysteine 474 and cysteine 652
Cysteine 794 and cysteine 803 L
Cysteine 466 and cysteine 474
Cysteine 466 and cysteine 652
Cysteine 609 and cysteine 652
Cysteine 474 and cysteine 609
A redox-regulated disulphide may form within Oxysterol-binding protein 1 between cysteines 474 and 652.

Details

Redox score ?
80
PDB code
7v62
Structure name
crystal structure of human osbp ord in complex with cholesterol
Structure deposition date
2021-08-19
Thiol separation (Å)
2
Half-sphere exposure sum ?
84
Minimum pKa ?
nan
% buried
nan
Peptide accession
P22059
Residue number A
474
Residue number B
652
Peptide name
Oxysterol-binding protein 1

Ligandability

Cysteine 474 of Oxysterol-binding 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 652 of Oxysterol-binding 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 Oxysterol-binding protein 1 between cysteines 794 and 803. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
7v62
Structure name
crystal structure of human osbp ord in complex with cholesterol
Structure deposition date
2021-08-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
43
Minimum pKa ?
10
% buried
36
Peptide accession
P22059
Residue number A
794
Residue number B
803
Peptide name
Oxysterol-binding protein 1

Ligandability

Cysteine 794 of Oxysterol-binding 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 803 of Oxysterol-binding 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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Oxysterol-binding protein 1 between cysteines 466 and 474. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
7v62
Structure name
crystal structure of human osbp ord in complex with cholesterol
Structure deposition date
2021-08-19
Thiol separation (Å)
8
Half-sphere exposure sum ?
72
Minimum pKa ?
11
% buried
nan
Peptide accession
P22059
Residue number A
466
Residue number B
474
Peptide name
Oxysterol-binding protein 1

Ligandability

Cysteine 466 of Oxysterol-binding 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 474 of Oxysterol-binding 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 Oxysterol-binding protein 1 between cysteines 466 and 652. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
7v62
Structure name
crystal structure of human osbp ord in complex with cholesterol
Structure deposition date
2021-08-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
60
Minimum pKa ?
10
% buried
nan
Peptide accession
P22059
Residue number A
466
Residue number B
652
Peptide name
Oxysterol-binding protein 1

Ligandability

Cysteine 466 of Oxysterol-binding 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 652 of Oxysterol-binding 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 Oxysterol-binding protein 1 between cysteines 609 and 652. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
7v62
Structure name
crystal structure of human osbp ord in complex with cholesterol
Structure deposition date
2021-08-19
Thiol separation (Å)
8
Half-sphere exposure sum ?
82
Minimum pKa ?
13
% buried
nan
Peptide accession
P22059
Residue number A
609
Residue number B
652
Peptide name
Oxysterol-binding protein 1

Ligandability

Cysteine 609 of Oxysterol-binding 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 652 of Oxysterol-binding 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 Oxysterol-binding protein 1 between cysteines 474 and 609. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
7v62
Structure name
crystal structure of human osbp ord in complex with cholesterol
Structure deposition date
2021-08-19
Thiol separation (Å)
8
Half-sphere exposure sum ?
90
Minimum pKa ?
13
% buried
nan
Peptide accession
P22059
Residue number A
474
Residue number B
609
Peptide name
Oxysterol-binding protein 1

Ligandability

Cysteine 474 of Oxysterol-binding 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 609 of Oxysterol-binding 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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