ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Diacylglycerol kinase delta

Intramolecular
Cysteine 249 and cysteine 252
Cysteine 249 and cysteine 278
Cysteine 267 and cysteine 286
Cysteine 267 and cysteine 270
Cysteine 249 and cysteine 256
Cysteine 270 and cysteine 286
Cysteine 252 and cysteine 278
Cysteine 252 and cysteine 256
Cysteine 256 and cysteine 278
A redox-regulated disulphide may form within Diacylglycerol kinase delta between cysteines 249 and 252 (41 and 44 respectively in this structure).

Details

Redox score ?
89
PDB code
1r79
Structure name
solution structure of the c1 domain of the human diacylglycerol kinase delta
Structure deposition date
2003-10-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
5
% buried
6
Peptide accession
Q16760
Residue number A
249
Residue number B
252
Peptide name
Diacylglycerol kinase delta

Ligandability

Cysteine 249 of Diacylglycerol kinase delta

Cysteine 252 of Diacylglycerol kinase delta

A redox-regulated disulphide may form within Diacylglycerol kinase delta between cysteines 249 and 278 (41 and 70 respectively in this structure).

Details

Redox score ?
88
PDB code
1r79
Structure name
solution structure of the c1 domain of the human diacylglycerol kinase delta
Structure deposition date
2003-10-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
5
% buried
6
Peptide accession
Q16760
Residue number A
249
Residue number B
278
Peptide name
Diacylglycerol kinase delta

Ligandability

Cysteine 249 of Diacylglycerol kinase delta

Cysteine 278 of Diacylglycerol kinase delta

A redox-regulated disulphide may form within Diacylglycerol kinase delta between cysteines 267 and 286 (59 and 78 respectively in this structure).

Details

Redox score ?
87
PDB code
1r79
Structure name
solution structure of the c1 domain of the human diacylglycerol kinase delta
Structure deposition date
2003-10-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
6
% buried
8
Peptide accession
Q16760
Residue number A
267
Residue number B
286
Peptide name
Diacylglycerol kinase delta

Ligandability

Cysteine 267 of Diacylglycerol kinase delta

Cysteine 286 of Diacylglycerol kinase delta

A redox-regulated disulphide may form within Diacylglycerol kinase delta between cysteines 267 and 270 (59 and 62 respectively in this structure).

Details

Redox score ?
87
PDB code
1r79
Structure name
solution structure of the c1 domain of the human diacylglycerol kinase delta
Structure deposition date
2003-10-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
6
% buried
16
Peptide accession
Q16760
Residue number A
267
Residue number B
270
Peptide name
Diacylglycerol kinase delta

Ligandability

Cysteine 267 of Diacylglycerol kinase delta

Cysteine 270 of Diacylglycerol kinase delta

A redox-regulated disulphide may form within Diacylglycerol kinase delta between cysteines 249 and 256 (41 and 48 respectively in this structure).

Details

Redox score ?
84
PDB code
1r79
Structure name
solution structure of the c1 domain of the human diacylglycerol kinase delta
Structure deposition date
2003-10-21
Thiol separation (Å)
5
Half-sphere exposure sum ?
58
Minimum pKa ?
5
% buried
14
Peptide accession
Q16760
Residue number A
249
Residue number B
256
Peptide name
Diacylglycerol kinase delta

Ligandability

Cysteine 249 of Diacylglycerol kinase delta

Cysteine 256 of Diacylglycerol kinase delta

A redox-regulated disulphide may form within Diacylglycerol kinase delta between cysteines 270 and 286 (62 and 78 respectively in this structure).

Details

Redox score ?
80
PDB code
1r79
Structure name
solution structure of the c1 domain of the human diacylglycerol kinase delta
Structure deposition date
2003-10-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
8
% buried
8
Peptide accession
Q16760
Residue number A
270
Residue number B
286
Peptide name
Diacylglycerol kinase delta

Ligandability

Cysteine 270 of Diacylglycerol kinase delta

Cysteine 286 of Diacylglycerol kinase delta

A redox-regulated disulphide may form within Diacylglycerol kinase delta between cysteines 252 and 278 (44 and 70 respectively in this structure).

Details

Redox score ?
80
PDB code
1r79
Structure name
solution structure of the c1 domain of the human diacylglycerol kinase delta
Structure deposition date
2003-10-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
41
Minimum pKa ?
9
% buried
0
Peptide accession
Q16760
Residue number A
252
Residue number B
278
Peptide name
Diacylglycerol kinase delta

Ligandability

Cysteine 252 of Diacylglycerol kinase delta

Cysteine 278 of Diacylglycerol kinase delta

A redox-regulated disulphide may form within Diacylglycerol kinase delta between cysteines 252 and 256 (44 and 48 respectively in this structure).

Details

Redox score ?
69
PDB code
1r79
Structure name
solution structure of the c1 domain of the human diacylglycerol kinase delta
Structure deposition date
2003-10-21
Thiol separation (Å)
6
Half-sphere exposure sum ?
49
Minimum pKa ?
9
% buried
8
Peptide accession
Q16760
Residue number A
252
Residue number B
256
Peptide name
Diacylglycerol kinase delta

Ligandability

Cysteine 252 of Diacylglycerol kinase delta

Cysteine 256 of Diacylglycerol kinase delta

A redox-regulated disulphide may form within Diacylglycerol kinase delta between cysteines 256 and 278 (48 and 70 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
60
PDB code
1r79
Structure name
solution structure of the c1 domain of the human diacylglycerol kinase delta
Structure deposition date
2003-10-21
Thiol separation (Å)
7
Half-sphere exposure sum ?
52
Minimum pKa ?
10
% buried
8
Peptide accession
Q16760
Residue number A
256
Residue number B
278
Peptide name
Diacylglycerol kinase delta

Ligandability

Cysteine 256 of Diacylglycerol kinase delta

Cysteine 278 of Diacylglycerol kinase delta

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