Protein kinase C alpha type
Intramolecular
Cysteine 132 and cysteine 151
Cysteine 115 and cysteine 118
Cysteine 132 and cysteine 135
Cysteine 115 and cysteine 143
Cysteine 135 and cysteine 151
Cysteine 118 and cysteine 143
Cysteine 383 and cysteine 485
Cysteine 383 and cysteine 499
2eli A 48 A 67
A redox-regulated disulphide may form within Protein kinase C alpha type between cysteines 132 and 151 (48 and 67 respectively in this structure).
Details
Redox score ?
91
PDB code
2eli
Structure name
solution structure of the second phorbol esters/diacylglycerol binding domain of human protein kinase c alpha type
Structure deposition date
2007-03-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
5
% buried
8
Peptide accession
P17252
Residue number A
132
Residue number B
151
Peptide name
Protein kinase C alpha type
Ligandability
Cysteine 132 of Protein kinase C alpha type
Cysteine 151 of Protein kinase C alpha type
2eli A 31 A 34
A redox-regulated disulphide may form within Protein kinase C alpha type between cysteines 115 and 118 (31 and 34 respectively in this structure).
Details
Redox score ?
90
PDB code
2eli
Structure name
solution structure of the second phorbol esters/diacylglycerol binding domain of human protein kinase c alpha type
Structure deposition date
2007-03-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
43
Minimum pKa ?
5
% buried
6
Peptide accession
P17252
Residue number A
115
Residue number B
118
Peptide name
Protein kinase C alpha type
Ligandability
Cysteine 115 of Protein kinase C alpha type
Cysteine 118 of Protein kinase C alpha type
2eli A 48 A 51
A redox-regulated disulphide may form within Protein kinase C alpha type between cysteines 132 and 135 (48 and 51 respectively in this structure).
Details
Redox score ?
89
PDB code
2eli
Structure name
solution structure of the second phorbol esters/diacylglycerol binding domain of human protein kinase c alpha type
Structure deposition date
2007-03-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
5
% buried
16
Peptide accession
P17252
Residue number A
132
Residue number B
135
Peptide name
Protein kinase C alpha type
Ligandability
Cysteine 132 of Protein kinase C alpha type
Cysteine 135 of Protein kinase C alpha type
2eli A 31 A 59
A redox-regulated disulphide may form within Protein kinase C alpha type between cysteines 115 and 143 (31 and 59 respectively in this structure).
Details
Redox score ?
89
PDB code
2eli
Structure name
solution structure of the second phorbol esters/diacylglycerol binding domain of human protein kinase c alpha type
Structure deposition date
2007-03-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
5
% buried
6
Peptide accession
P17252
Residue number A
115
Residue number B
143
Peptide name
Protein kinase C alpha type
Ligandability
Cysteine 115 of Protein kinase C alpha type
Cysteine 143 of Protein kinase C alpha type
2eli A 51 A 67
A redox-regulated disulphide may form within Protein kinase C alpha type between cysteines 135 and 151 (51 and 67 respectively in this structure).
Details
Redox score ?
80
PDB code
2eli
Structure name
solution structure of the second phorbol esters/diacylglycerol binding domain of human protein kinase c alpha type
Structure deposition date
2007-03-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
9
% buried
10
Peptide accession
P17252
Residue number A
135
Residue number B
151
Peptide name
Protein kinase C alpha type
Ligandability
Cysteine 135 of Protein kinase C alpha type
Cysteine 151 of Protein kinase C alpha type
2eli A 34 A 59
A redox-regulated disulphide may form within Protein kinase C alpha type between cysteines 118 and 143 (34 and 59 respectively in this structure).
Details
Redox score ?
80
PDB code
2eli
Structure name
solution structure of the second phorbol esters/diacylglycerol binding domain of human protein kinase c alpha type
Structure deposition date
2007-03-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
41
Minimum pKa ?
8
% buried
0
Peptide accession
P17252
Residue number A
118
Residue number B
143
Peptide name
Protein kinase C alpha type
Ligandability
Cysteine 118 of Protein kinase C alpha type
Cysteine 143 of Protein kinase C alpha type
3iw4 C 383 C 485
A redox-regulated disulphide may form within Protein kinase C alpha type between cysteines 383 and 485. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
33
PDB code
3iw4
Structure name
crystal structure of pkc alpha in complex with nvp-aeb071
Structure deposition date
2009-09-02
Thiol separation (Å)
10
Half-sphere exposure sum ?
63
Minimum pKa ?
11
% buried
76
Peptide accession
P17252
Residue number A
383
Residue number B
485
Peptide name
Protein kinase C alpha type
Ligandability
Cysteine 383 of Protein kinase C alpha type
Cysteine 485 of Protein kinase C alpha type
3iw4 B 383 B 499
A redox-regulated disulphide may form within Protein kinase C alpha type between cysteines 383 and 499. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
32
PDB code
3iw4
Structure name
crystal structure of pkc alpha in complex with nvp-aeb071
Structure deposition date
2009-09-02
Thiol separation (Å)
10
Half-sphere exposure sum ?
57
Minimum pKa ?
11
% buried
64
Peptide accession
P17252
Residue number A
383
Residue number B
499
Peptide name
Protein kinase C alpha type
Ligandability
Cysteine 383 of Protein kinase C alpha type
Cysteine 499 of Protein kinase C alpha type
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