ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

DnaJ homolog subfamily C member 24

Intramolecular
Cysteine 115 and cysteine 136
Cysteine 115 and cysteine 117
Cysteine 136 and cysteine 139
Cysteine 117 and cysteine 136
Cysteine 117 and cysteine 139
Cysteine 115 and cysteine 139
Cysteine 83 and cysteine 117
A redox-regulated disulphide may form within DnaJ homolog subfamily C member 24 between cysteines 115 and 136.

Details

Redox score ?
87
PDB code
2l6l
Structure name
solution structure of human j-protein co-chaperone, dph4
Structure deposition date
2010-11-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
8
% buried
2
Peptide accession
Q6P3W2
Residue number A
115
Residue number B
136
Peptide name
DnaJ homolog subfamily C member 24

Ligandability

Cysteine 115 of DnaJ homolog subfamily C member 24

Cysteine 136 of DnaJ homolog subfamily C member 24

A redox-regulated disulphide may form within DnaJ homolog subfamily C member 24 between cysteines 115 and 117.

Details

Redox score ?
86
PDB code
2l6l
Structure name
solution structure of human j-protein co-chaperone, dph4
Structure deposition date
2010-11-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
36
Minimum pKa ?
8
% buried
1
Peptide accession
Q6P3W2
Residue number A
115
Residue number B
117
Peptide name
DnaJ homolog subfamily C member 24

Ligandability

Cysteine 115 of DnaJ homolog subfamily C member 24

Cysteine 117 of DnaJ homolog subfamily C member 24

A redox-regulated disulphide may form within DnaJ homolog subfamily C member 24 between cysteines 136 and 139.

Details

Redox score ?
85
PDB code
2l6l
Structure name
solution structure of human j-protein co-chaperone, dph4
Structure deposition date
2010-11-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
42
Minimum pKa ?
8
% buried
0
Peptide accession
Q6P3W2
Residue number A
136
Residue number B
139
Peptide name
DnaJ homolog subfamily C member 24

Ligandability

Cysteine 136 of DnaJ homolog subfamily C member 24

Cysteine 139 of DnaJ homolog subfamily C member 24

A redox-regulated disulphide may form within DnaJ homolog subfamily C member 24 between cysteines 117 and 136.

Details

Redox score ?
85
PDB code
2l6l
Structure name
solution structure of human j-protein co-chaperone, dph4
Structure deposition date
2010-11-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
38
Minimum pKa ?
8
% buried
0
Peptide accession
Q6P3W2
Residue number A
117
Residue number B
136
Peptide name
DnaJ homolog subfamily C member 24

Ligandability

Cysteine 117 of DnaJ homolog subfamily C member 24

Cysteine 136 of DnaJ homolog subfamily C member 24

A redox-regulated disulphide may form within DnaJ homolog subfamily C member 24 between cysteines 117 and 139.

Details

Redox score ?
85
PDB code
2l6l
Structure name
solution structure of human j-protein co-chaperone, dph4
Structure deposition date
2010-11-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
28
Minimum pKa ?
8
% buried
0
Peptide accession
Q6P3W2
Residue number A
117
Residue number B
139
Peptide name
DnaJ homolog subfamily C member 24

Ligandability

Cysteine 117 of DnaJ homolog subfamily C member 24

Cysteine 139 of DnaJ homolog subfamily C member 24

A redox-regulated disulphide may form within DnaJ homolog subfamily C member 24 between cysteines 115 and 139.

Details

Redox score ?
83
PDB code
2l6l
Structure name
solution structure of human j-protein co-chaperone, dph4
Structure deposition date
2010-11-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
40
Minimum pKa ?
9
% buried
1
Peptide accession
Q6P3W2
Residue number A
115
Residue number B
139
Peptide name
DnaJ homolog subfamily C member 24

Ligandability

Cysteine 115 of DnaJ homolog subfamily C member 24

Cysteine 139 of DnaJ homolog subfamily C member 24

A redox-regulated disulphide may form within DnaJ homolog subfamily C member 24 between cysteines 83 and 117. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
2l6l
Structure name
solution structure of human j-protein co-chaperone, dph4
Structure deposition date
2010-11-23
Thiol separation (Å)
9
Half-sphere exposure sum ?
29
Minimum pKa ?
8
% buried
0
Peptide accession
Q6P3W2
Residue number A
83
Residue number B
117
Peptide name
DnaJ homolog subfamily C member 24

Ligandability

Cysteine 83 of DnaJ homolog subfamily C member 24

Cysteine 117 of DnaJ homolog subfamily C member 24

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