ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Transcription factor p65

Intermolecular
Cysteine 197 and cysteine 240 of NF-kappa-B inhibitor beta
Intramolecular
Cysteine 197 and cysteine 216
Cysteine 105 and cysteine 109
Cysteine 38 and cysteine 120 L
A redox-regulated disulphide may form between cysteine 197 of Transcription factor p65 and cysteine 240 of NF-kappa-B inhibitor beta. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
PDB code
1k3z
Structure name
x-ray crystal structure of the ikbb/nf-kb p65 homodimer complex
Structure deposition date
2001-10-04
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
12
% buried
95
Peptide A name
Transcription factor p65
Peptide B name
NF-kappa-B inhibitor beta
Peptide A accession
Q04207
Peptide B accession
Q60778
Peptide A residue number
197
Peptide B residue number
240

Ligandability

Cysteine 197 of Transcription factor p65

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 240 of NF-kappa-B inhibitor beta

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Transcription factor p65 between cysteines 197 and 216. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
3gut
Structure name
crystal structure of a higher-order complex of p50:rela bound to the hiv-1 ltr
Structure deposition date
2009-03-30
Thiol separation (Å)
7
Half-sphere exposure sum ?
62
Minimum pKa ?
11
% buried
78
Peptide accession
Q04206
Residue number A
197
Residue number B
216
Peptide name
Transcription factor p65

Ligandability

Cysteine 197 of Transcription factor p65

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 216 of Transcription factor p65

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Transcription factor p65 between cysteines 105 and 109. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
1nfi
Structure name
i-kappa-b-alpha/nf-kappa-b complex
Structure deposition date
1998-08-25
Thiol separation (Å)
9
Half-sphere exposure sum ?
54
Minimum pKa ?
9
% buried
11
Peptide accession
Q04206
Residue number A
105
Residue number B
109
Peptide name
Transcription factor p65

Ligandability

Cysteine 105 of Transcription factor p65

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 109 of Transcription factor p65

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Transcription factor p65 between cysteines 38 and 120. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
1ikn
Structure name
ikappabalpha/nf-kappab complex
Structure deposition date
1998-11-13
Thiol separation (Å)
8
Half-sphere exposure sum ?
48
Minimum pKa ?
9
% buried
22
Peptide accession
Q04207
Residue number A
38
Residue number B
120
Peptide name
Transcription factor p65

Ligandability

Cysteine 38 of Transcription factor p65

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 120 of Transcription factor p65

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

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