ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Protein kinase C beta type

Intramolecular
Cysteine 132 and cysteine 135
Cysteine 135 and cysteine 151
Cysteine 115 and cysteine 118
Cysteine 118 and cysteine 143
Cysteine 115 and cysteine 143
Cysteine 132 and cysteine 151
Cysteine 488 and cysteine 502
A redox-regulated disulphide may form within Protein kinase C beta type between cysteines 132 and 135.

Details

Redox score ?
84
PDB code
3pfq
Structure name
crystal structure and allosteric activation of protein kinase c beta ii
Structure deposition date
2010-10-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
44
Minimum pKa ?
7
% buried
9
Peptide accession
P68403
Residue number A
132
Residue number B
135
Peptide name
Protein kinase C beta type

Ligandability

Cysteine 132 of Protein kinase C beta type

Cysteine 135 of Protein kinase C beta type

A redox-regulated disulphide may form within Protein kinase C beta type between cysteines 135 and 151.

Details

Redox score ?
77
PDB code
3pfq
Structure name
crystal structure and allosteric activation of protein kinase c beta ii
Structure deposition date
2010-10-28
Thiol separation (Å)
5
Half-sphere exposure sum ?
36
Minimum pKa ?
7
% buried
0
Peptide accession
P68403
Residue number A
135
Residue number B
151
Peptide name
Protein kinase C beta type

Ligandability

Cysteine 135 of Protein kinase C beta type

Cysteine 151 of Protein kinase C beta type

A redox-regulated disulphide may form within Protein kinase C beta type between cysteines 115 and 118.

Details

Redox score ?
75
PDB code
3pfq
Structure name
crystal structure and allosteric activation of protein kinase c beta ii
Structure deposition date
2010-10-28
Thiol separation (Å)
5
Half-sphere exposure sum ?
47
Minimum pKa ?
7
% buried
11
Peptide accession
P68403
Residue number A
115
Residue number B
118
Peptide name
Protein kinase C beta type

Ligandability

Cysteine 115 of Protein kinase C beta type

Cysteine 118 of Protein kinase C beta type

A redox-regulated disulphide may form within Protein kinase C beta type between cysteines 118 and 143.

Details

Redox score ?
72
PDB code
3pfq
Structure name
crystal structure and allosteric activation of protein kinase c beta ii
Structure deposition date
2010-10-28
Thiol separation (Å)
5
Half-sphere exposure sum ?
45
Minimum pKa ?
8
% buried
4
Peptide accession
P68403
Residue number A
118
Residue number B
143
Peptide name
Protein kinase C beta type

Ligandability

Cysteine 118 of Protein kinase C beta type

Cysteine 143 of Protein kinase C beta type

A redox-regulated disulphide may form within Protein kinase C beta type between cysteines 115 and 143.

Details

Redox score ?
72
PDB code
3pfq
Structure name
crystal structure and allosteric activation of protein kinase c beta ii
Structure deposition date
2010-10-28
Thiol separation (Å)
6
Half-sphere exposure sum ?
52
Minimum pKa ?
7
% buried
14
Peptide accession
P68403
Residue number A
115
Residue number B
143
Peptide name
Protein kinase C beta type

Ligandability

Cysteine 115 of Protein kinase C beta type

Cysteine 143 of Protein kinase C beta type

A redox-regulated disulphide may form within Protein kinase C beta type between cysteines 132 and 151. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
3pfq
Structure name
crystal structure and allosteric activation of protein kinase c beta ii
Structure deposition date
2010-10-28
Thiol separation (Å)
8
Half-sphere exposure sum ?
44
Minimum pKa ?
9
% buried
9
Peptide accession
P68403
Residue number A
132
Residue number B
151
Peptide name
Protein kinase C beta type

Ligandability

Cysteine 132 of Protein kinase C beta type

Cysteine 151 of Protein kinase C beta type

A redox-regulated disulphide may form within Protein kinase C beta type between cysteines 488 and 502. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
3pfq
Structure name
crystal structure and allosteric activation of protein kinase c beta ii
Structure deposition date
2010-10-28
Thiol separation (Å)
10
Half-sphere exposure sum ?
60
Minimum pKa ?
10
% buried
86
Peptide accession
P68403
Residue number A
488
Residue number B
502
Peptide name
Protein kinase C beta type

Ligandability

Cysteine 488 of Protein kinase C beta type

Cysteine 502 of Protein kinase C beta type

If this tool was useful for finding a disulphide, please cite: