ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Transcription factor RelB

Intramolecular
Cysteine 181 and cysteine 186
Cysteine 284 and cysteine 303
Cysteine 161 and cysteine 247
Cysteine 161 and cysteine 181
Cysteine 122 and cysteine 207 L
Cysteine 161 and cysteine 186
A redox-regulated disulphide may form within Transcription factor RelB between cysteines 181 and 186.

Details

Redox score ?
86
PDB code
3do7
Structure name
x-ray structure of a nf-kb p52/relb/dna complex
Structure deposition date
2008-07-03
Thiol separation (Å)
3
Half-sphere exposure sum ?
61
Minimum pKa ?
8
% buried
58
Peptide accession
Q8VE46
Residue number A
181
Residue number B
186
Peptide name
Transcription factor RelB

Ligandability

Cysteine 181 of Transcription factor RelB

Cysteine 186 of Transcription factor RelB

A redox-regulated disulphide may form within Transcription factor RelB between cysteines 284 and 303. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
3do7
Structure name
x-ray structure of a nf-kb p52/relb/dna complex
Structure deposition date
2008-07-03
Thiol separation (Å)
7
Half-sphere exposure sum ?
62
Minimum pKa ?
11
% buried
76
Peptide accession
Q8VE46
Residue number A
284
Residue number B
303
Peptide name
Transcription factor RelB

Ligandability

Cysteine 284 of Transcription factor RelB

Cysteine 303 of Transcription factor RelB

A redox-regulated disulphide may form within Transcription factor RelB between cysteines 161 and 247. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
2v2t
Structure name
x-ray structure of a nf-kb p50-relb-dna complex
Structure deposition date
2007-06-07
Thiol separation (Å)
7
Half-sphere exposure sum ?
88
Minimum pKa ?
11
% buried
86
Peptide accession
Q04863
Residue number A
161
Residue number B
247
Peptide name
Transcription factor RelB

Ligandability

Cysteine 161 of Transcription factor RelB

Cysteine 247 of Transcription factor RelB

A redox-regulated disulphide may form within Transcription factor RelB between cysteines 161 and 181. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
2v2t
Structure name
x-ray structure of a nf-kb p50-relb-dna complex
Structure deposition date
2007-06-07
Thiol separation (Å)
10
Half-sphere exposure sum ?
72
Minimum pKa ?
8
% buried
72
Peptide accession
Q04863
Residue number A
161
Residue number B
181
Peptide name
Transcription factor RelB

Ligandability

Cysteine 161 of Transcription factor RelB

Cysteine 181 of Transcription factor RelB

A redox-regulated disulphide may form within Transcription factor RelB between cysteines 122 and 207. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
2v2t
Structure name
x-ray structure of a nf-kb p50-relb-dna complex
Structure deposition date
2007-06-07
Thiol separation (Å)
8
Half-sphere exposure sum ?
51
Minimum pKa ?
11
% buried
74
Peptide accession
Q04863
Residue number A
122
Residue number B
207
Peptide name
Transcription factor RelB

Ligandability

Cysteine 122 of Transcription factor RelB

Cysteine 207 of Transcription factor RelB

A redox-regulated disulphide may form within Transcription factor RelB between cysteines 161 and 186. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
2v2t
Structure name
x-ray structure of a nf-kb p50-relb-dna complex
Structure deposition date
2007-06-07
Thiol separation (Å)
8
Half-sphere exposure sum ?
79
Minimum pKa ?
12
% buried
86
Peptide accession
Q04863
Residue number A
161
Residue number B
186
Peptide name
Transcription factor RelB

Ligandability

Cysteine 161 of Transcription factor RelB

Cysteine 186 of Transcription factor RelB

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