ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1

Intramolecular
Cysteine 608 and cysteine 646 L
Cysteine 368 and cysteine 417
Cysteine 356 and cysteine 361
Cysteine 361 and cysteine 363
Cysteine 363 and cysteine 960
Cysteine 1088 and cysteine 1091
Cysteine 318 and cysteine 1060
A redox-regulated disulphide may form within 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 between cysteines 608 and 646.

Details

Redox score ?
82
PDB code
4ey0
Structure name
structure of tandem sh2 domains from plcgamma1
Structure deposition date
2012-05-01
Thiol separation (Å)
3
Half-sphere exposure sum ?
57
Minimum pKa ?
7
% buried
68
Peptide accession
P19174
Residue number A
608
Residue number B
646
Peptide name
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1

Ligandability

Cysteine 608 of 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-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 646 of 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-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.

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 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 between cysteines 368 and 417. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
6pbc
Structure name
structural basis for the activation of plc-gamma isozymes by phosphorylation and cancer-associated mutations
Structure deposition date
2019-06-13
Thiol separation (Å)
5
Half-sphere exposure sum ?
68
Minimum pKa ?
14
% buried
81
Peptide accession
P10686
Residue number A
368
Residue number B
417
Peptide name
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1

Ligandability

Cysteine 368 of 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-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 417 of 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-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 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 between cysteines 356 and 361. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
6pbc
Structure name
structural basis for the activation of plc-gamma isozymes by phosphorylation and cancer-associated mutations
Structure deposition date
2019-06-13
Thiol separation (Å)
5
Half-sphere exposure sum ?
99
Minimum pKa ?
13
% buried
100
Peptide accession
P10686
Residue number A
356
Residue number B
361
Peptide name
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1

Ligandability

Cysteine 356 of 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-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 361 of 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-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 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 between cysteines 361 and 363. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
6pbc
Structure name
structural basis for the activation of plc-gamma isozymes by phosphorylation and cancer-associated mutations
Structure deposition date
2019-06-13
Thiol separation (Å)
7
Half-sphere exposure sum ?
92
Minimum pKa ?
11
% buried
100
Peptide accession
P10686
Residue number A
361
Residue number B
363
Peptide name
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1

Ligandability

Cysteine 361 of 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-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 363 of 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-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 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 between cysteines 363 and 960. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
6pbc
Structure name
structural basis for the activation of plc-gamma isozymes by phosphorylation and cancer-associated mutations
Structure deposition date
2019-06-13
Thiol separation (Å)
7
Half-sphere exposure sum ?
85
Minimum pKa ?
11
% buried
100
Peptide accession
P10686
Residue number A
363
Residue number B
960
Peptide name
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1

Ligandability

Cysteine 363 of 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-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 960 of 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-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 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 between cysteines 1088 and 1091. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
6pbc
Structure name
structural basis for the activation of plc-gamma isozymes by phosphorylation and cancer-associated mutations
Structure deposition date
2019-06-13
Thiol separation (Å)
10
Half-sphere exposure sum ?
56
Minimum pKa ?
10
% buried
31
Peptide accession
P10686
Residue number A
1088
Residue number B
1091
Peptide name
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1

Ligandability

Cysteine 1088 of 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-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 1091 of 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-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 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 between cysteines 318 and 1060. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
6pbc
Structure name
structural basis for the activation of plc-gamma isozymes by phosphorylation and cancer-associated mutations
Structure deposition date
2019-06-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
10
% buried
42
Peptide accession
P10686
Residue number A
318
Residue number B
1060
Peptide name
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1

Ligandability

Cysteine 318 of 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-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 1060 of 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-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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