ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Phosphatidylinositol 3-kinase catalytic subunit type 3

Intramolecular
Cysteine 733 and cysteine 802
Cysteine 729 and cysteine 733
Cysteine 729 and cysteine 802
A redox-regulated disulphide may form within Phosphatidylinositol 3-kinase catalytic subunit type 3 between cysteines 733 and 802.

Details

Redox score ?
65
PDB code
3ihy
Structure name
human pik3c3 crystal structure
Structure deposition date
2009-07-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
81
Minimum pKa ?
9
% buried
100
Peptide accession
Q8NEB9
Residue number A
733
Residue number B
802
Peptide name
Phosphatidylinositol 3-kinase catalytic subunit type 3

Ligandability

Cysteine 733 of Phosphatidylinositol 3-kinase catalytic subunit type 3

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 802 of Phosphatidylinositol 3-kinase catalytic subunit type 3

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 Phosphatidylinositol 3-kinase catalytic subunit type 3 between cysteines 729 and 733. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
7rsv
Structure name
structure of the vps34 kinase domain with compound 5
Structure deposition date
2021-08-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
87
Minimum pKa ?
11
% buried
100
Peptide accession
Q8NEB9
Residue number A
729
Residue number B
733
Peptide name
Phosphatidylinositol 3-kinase catalytic subunit type 3

Ligandability

Cysteine 729 of Phosphatidylinositol 3-kinase catalytic subunit type 3

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 733 of Phosphatidylinositol 3-kinase catalytic subunit type 3

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 Phosphatidylinositol 3-kinase catalytic subunit type 3 between cysteines 729 and 802. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
29
PDB code
3ihy
Structure name
human pik3c3 crystal structure
Structure deposition date
2009-07-31
Thiol separation (Å)
9
Half-sphere exposure sum ?
83
Minimum pKa ?
13
% buried
100
Peptide accession
Q8NEB9
Residue number A
729
Residue number B
802
Peptide name
Phosphatidylinositol 3-kinase catalytic subunit type 3

Ligandability

Cysteine 729 of Phosphatidylinositol 3-kinase catalytic subunit type 3

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 802 of Phosphatidylinositol 3-kinase catalytic subunit type 3

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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