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
3do7 A 181 A 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
3do7 A 284 A 303
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
2v2t A 161 A 247
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
2v2t A 161 A 181
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
2v2t A 122 A 207
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
2v2t A 161 A 186
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: