ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Vacuolar protein sorting-associated protein 35

Intramolecular
Cysteine 653 and cysteine 673
Cysteine 673 and cysteine 699
Cysteine 653 and cysteine 699
A redox-regulated disulphide may form within Vacuolar protein sorting-associated protein 35 between cysteines 653 and 673.

Details

Redox score ?
63
PDB code
5osh
Structure name
structure of retromer vps29-vps35c subunits complexed with ridl n- terminal domain (1-236)
Structure deposition date
2017-08-17
Thiol separation (Å)
5
Half-sphere exposure sum ?
87
Minimum pKa ?
9
% buried
100
Peptide accession
Q96QK1
Residue number A
653
Residue number B
673
Peptide name
Vacuolar protein sorting-associated protein 35

Ligandability

Cysteine 653 of Vacuolar protein sorting-associated protein 35

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 673 of Vacuolar protein sorting-associated protein 35

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 Vacuolar protein sorting-associated protein 35 between cysteines 673 and 699. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
2r17
Structure name
functional architecture of the retromer cargo-recognition complex
Structure deposition date
2007-08-22
Thiol separation (Å)
6
Half-sphere exposure sum ?
77
Minimum pKa ?
11
% buried
82
Peptide accession
Q96QK1
Residue number A
673
Residue number B
699
Peptide name
Vacuolar protein sorting-associated protein 35

Ligandability

Cysteine 673 of Vacuolar protein sorting-associated protein 35

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 699 of Vacuolar protein sorting-associated protein 35

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 Vacuolar protein sorting-associated protein 35 between cysteines 653 and 699. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
2r17
Structure name
functional architecture of the retromer cargo-recognition complex
Structure deposition date
2007-08-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
75
Minimum pKa ?
11
% buried
82
Peptide accession
Q96QK1
Residue number A
653
Residue number B
699
Peptide name
Vacuolar protein sorting-associated protein 35

Ligandability

Cysteine 653 of Vacuolar protein sorting-associated protein 35

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 699 of Vacuolar protein sorting-associated protein 35

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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