ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

DnaJ homolog subfamily A member 3, mitochondrial

Intramolecular
Cysteine 275 and cysteine 278
Cysteine 256 and cysteine 278
Cysteine 236 and cysteine 239
Cysteine 253 and cysteine 256
Cysteine 239 and cysteine 292
Cysteine 256 and cysteine 275
Cysteine 253 and cysteine 278
Cysteine 239 and cysteine 289
Cysteine 289 and cysteine 292
Cysteine 236 and cysteine 289
More...
Cysteine 253 and cysteine 275
Cysteine 236 and cysteine 292
A redox-regulated disulphide may form within DnaJ homolog subfamily A member 3, mitochondrial between cysteines 275 and 278 (70 and 73 respectively in this structure).

Details

Redox score ?
92
PDB code
2ctt
Structure name
solution structure of zinc finger domain from human dnaj subfamily a menber 3
Structure deposition date
2005-05-24
Thiol separation (Å)
3
Half-sphere exposure sum ?
55
Minimum pKa ?
6
% buried
0
Peptide accession
Q96EY1
Residue number A
275
Residue number B
278
Peptide name
DnaJ homolog subfamily A member 3, mitochondrial

Ligandability

Cysteine 275 of DnaJ homolog subfamily A member 3, mitochondrial

Cysteine 278 of DnaJ homolog subfamily A member 3, mitochondrial

A redox-regulated disulphide may form within DnaJ homolog subfamily A member 3, mitochondrial between cysteines 256 and 278 (51 and 73 respectively in this structure).

Details

Redox score ?
92
PDB code
2ctt
Structure name
solution structure of zinc finger domain from human dnaj subfamily a menber 3
Structure deposition date
2005-05-24
Thiol separation (Å)
3
Half-sphere exposure sum ?
55
Minimum pKa ?
5
% buried
0
Peptide accession
Q96EY1
Residue number A
256
Residue number B
278
Peptide name
DnaJ homolog subfamily A member 3, mitochondrial

Ligandability

Cysteine 256 of DnaJ homolog subfamily A member 3, mitochondrial

Cysteine 278 of DnaJ homolog subfamily A member 3, mitochondrial

A redox-regulated disulphide may form within DnaJ homolog subfamily A member 3, mitochondrial between cysteines 236 and 239 (31 and 34 respectively in this structure).

Details

Redox score ?
91
PDB code
2ctt
Structure name
solution structure of zinc finger domain from human dnaj subfamily a menber 3
Structure deposition date
2005-05-24
Thiol separation (Å)
3
Half-sphere exposure sum ?
53
Minimum pKa ?
6
% buried
0
Peptide accession
Q96EY1
Residue number A
236
Residue number B
239
Peptide name
DnaJ homolog subfamily A member 3, mitochondrial

Ligandability

Cysteine 236 of DnaJ homolog subfamily A member 3, mitochondrial

Cysteine 239 of DnaJ homolog subfamily A member 3, mitochondrial

A redox-regulated disulphide may form within DnaJ homolog subfamily A member 3, mitochondrial between cysteines 253 and 256 (48 and 51 respectively in this structure).

Details

Redox score ?
90
PDB code
2ctt
Structure name
solution structure of zinc finger domain from human dnaj subfamily a menber 3
Structure deposition date
2005-05-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
5
% buried
0
Peptide accession
Q96EY1
Residue number A
253
Residue number B
256
Peptide name
DnaJ homolog subfamily A member 3, mitochondrial

Ligandability

Cysteine 253 of DnaJ homolog subfamily A member 3, mitochondrial

Cysteine 256 of DnaJ homolog subfamily A member 3, mitochondrial

A redox-regulated disulphide may form within DnaJ homolog subfamily A member 3, mitochondrial between cysteines 239 and 292 (34 and 87 respectively in this structure).

Details

Redox score ?
90
PDB code
2ctt
Structure name
solution structure of zinc finger domain from human dnaj subfamily a menber 3
Structure deposition date
2005-05-24
Thiol separation (Å)
3
Half-sphere exposure sum ?
52
Minimum pKa ?
6
% buried
0
Peptide accession
Q96EY1
Residue number A
239
Residue number B
292
Peptide name
DnaJ homolog subfamily A member 3, mitochondrial

Ligandability

Cysteine 239 of DnaJ homolog subfamily A member 3, mitochondrial

Cysteine 292 of DnaJ homolog subfamily A member 3, mitochondrial

A redox-regulated disulphide may form within DnaJ homolog subfamily A member 3, mitochondrial between cysteines 256 and 275 (51 and 70 respectively in this structure).

Details

Redox score ?
90
PDB code
2ctt
Structure name
solution structure of zinc finger domain from human dnaj subfamily a menber 3
Structure deposition date
2005-05-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
5
% buried
0
Peptide accession
Q96EY1
Residue number A
256
Residue number B
275
Peptide name
DnaJ homolog subfamily A member 3, mitochondrial

Ligandability

Cysteine 256 of DnaJ homolog subfamily A member 3, mitochondrial

Cysteine 275 of DnaJ homolog subfamily A member 3, mitochondrial

A redox-regulated disulphide may form within DnaJ homolog subfamily A member 3, mitochondrial between cysteines 253 and 278 (48 and 73 respectively in this structure).

Details

Redox score ?
89
PDB code
2ctt
Structure name
solution structure of zinc finger domain from human dnaj subfamily a menber 3
Structure deposition date
2005-05-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
6
% buried
0
Peptide accession
Q96EY1
Residue number A
253
Residue number B
278
Peptide name
DnaJ homolog subfamily A member 3, mitochondrial

Ligandability

Cysteine 253 of DnaJ homolog subfamily A member 3, mitochondrial

Cysteine 278 of DnaJ homolog subfamily A member 3, mitochondrial

A redox-regulated disulphide may form within DnaJ homolog subfamily A member 3, mitochondrial between cysteines 239 and 289 (34 and 84 respectively in this structure).

Details

Redox score ?
88
PDB code
2ctt
Structure name
solution structure of zinc finger domain from human dnaj subfamily a menber 3
Structure deposition date
2005-05-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
6
% buried
0
Peptide accession
Q96EY1
Residue number A
239
Residue number B
289
Peptide name
DnaJ homolog subfamily A member 3, mitochondrial

Ligandability

Cysteine 239 of DnaJ homolog subfamily A member 3, mitochondrial

Cysteine 289 of DnaJ homolog subfamily A member 3, mitochondrial

A redox-regulated disulphide may form within DnaJ homolog subfamily A member 3, mitochondrial between cysteines 289 and 292 (84 and 87 respectively in this structure).

Details

Redox score ?
87
PDB code
2ctt
Structure name
solution structure of zinc finger domain from human dnaj subfamily a menber 3
Structure deposition date
2005-05-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
7
% buried
0
Peptide accession
Q96EY1
Residue number A
289
Residue number B
292
Peptide name
DnaJ homolog subfamily A member 3, mitochondrial

Ligandability

Cysteine 289 of DnaJ homolog subfamily A member 3, mitochondrial

Cysteine 292 of DnaJ homolog subfamily A member 3, mitochondrial

A redox-regulated disulphide may form within DnaJ homolog subfamily A member 3, mitochondrial between cysteines 236 and 289 (31 and 84 respectively in this structure).

Details

Redox score ?
86
PDB code
2ctt
Structure name
solution structure of zinc finger domain from human dnaj subfamily a menber 3
Structure deposition date
2005-05-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
7
% buried
0
Peptide accession
Q96EY1
Residue number A
236
Residue number B
289
Peptide name
DnaJ homolog subfamily A member 3, mitochondrial

Ligandability

Cysteine 236 of DnaJ homolog subfamily A member 3, mitochondrial

Cysteine 289 of DnaJ homolog subfamily A member 3, mitochondrial

A redox-regulated disulphide may form within DnaJ homolog subfamily A member 3, mitochondrial between cysteines 253 and 275 (48 and 70 respectively in this structure).

Details

Redox score ?
85
PDB code
2ctt
Structure name
solution structure of zinc finger domain from human dnaj subfamily a menber 3
Structure deposition date
2005-05-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
8
% buried
0
Peptide accession
Q96EY1
Residue number A
253
Residue number B
275
Peptide name
DnaJ homolog subfamily A member 3, mitochondrial

Ligandability

Cysteine 253 of DnaJ homolog subfamily A member 3, mitochondrial

Cysteine 275 of DnaJ homolog subfamily A member 3, mitochondrial

A redox-regulated disulphide may form within DnaJ homolog subfamily A member 3, mitochondrial between cysteines 236 and 292 (31 and 87 respectively in this structure).

Details

Redox score ?
84
PDB code
2ctt
Structure name
solution structure of zinc finger domain from human dnaj subfamily a menber 3
Structure deposition date
2005-05-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
7
% buried
0
Peptide accession
Q96EY1
Residue number A
236
Residue number B
292
Peptide name
DnaJ homolog subfamily A member 3, mitochondrial

Ligandability

Cysteine 236 of DnaJ homolog subfamily A member 3, mitochondrial

Cysteine 292 of DnaJ homolog subfamily A member 3, mitochondrial

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