ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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TNF receptor-associated factor 4

Intramolecular
Cysteine 195 and cysteine 214
Cysteine 195 and cysteine 198
Cysteine 221 and cysteine 243
Cysteine 221 and cysteine 225
Cysteine 225 and cysteine 243
Cysteine 198 and cysteine 214
A redox-regulated disulphide may form within TNF receptor-associated factor 4 between cysteines 195 and 214.

Details

Redox score ?
91
PDB code
2eod
Structure name
solution structure of traf-type zinc finger domains (190- 248) from human tnf receptor-associated factor 4
Structure deposition date
2007-03-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
5
% buried
0
Peptide accession
Q9BUZ4
Residue number A
195
Residue number B
214
Peptide name
TNF receptor-associated factor 4

Ligandability

Cysteine 195 of TNF receptor-associated factor 4

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 214 of TNF receptor-associated factor 4

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 TNF receptor-associated factor 4 between cysteines 195 and 198.

Details

Redox score ?
90
PDB code
2eod
Structure name
solution structure of traf-type zinc finger domains (190- 248) from human tnf receptor-associated factor 4
Structure deposition date
2007-03-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
5
% buried
0
Peptide accession
Q9BUZ4
Residue number A
195
Residue number B
198
Peptide name
TNF receptor-associated factor 4

Ligandability

Cysteine 195 of TNF receptor-associated factor 4

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 198 of TNF receptor-associated factor 4

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 TNF receptor-associated factor 4 between cysteines 221 and 243.

Details

Redox score ?
89
PDB code
2eod
Structure name
solution structure of traf-type zinc finger domains (190- 248) from human tnf receptor-associated factor 4
Structure deposition date
2007-03-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
7
% buried
0
Peptide accession
Q9BUZ4
Residue number A
221
Residue number B
243
Peptide name
TNF receptor-associated factor 4

Ligandability

Cysteine 221 of TNF receptor-associated factor 4

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 243 of TNF receptor-associated factor 4

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 TNF receptor-associated factor 4 between cysteines 221 and 225.

Details

Redox score ?
88
PDB code
2eod
Structure name
solution structure of traf-type zinc finger domains (190- 248) from human tnf receptor-associated factor 4
Structure deposition date
2007-03-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
44
Minimum pKa ?
7
% buried
0
Peptide accession
Q9BUZ4
Residue number A
221
Residue number B
225
Peptide name
TNF receptor-associated factor 4

Ligandability

Cysteine 221 of TNF receptor-associated factor 4

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 225 of TNF receptor-associated factor 4

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 TNF receptor-associated factor 4 between cysteines 225 and 243.

Details

Redox score ?
88
PDB code
2eod
Structure name
solution structure of traf-type zinc finger domains (190- 248) from human tnf receptor-associated factor 4
Structure deposition date
2007-03-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
43
Minimum pKa ?
7
% buried
0
Peptide accession
Q9BUZ4
Residue number A
225
Residue number B
243
Peptide name
TNF receptor-associated factor 4

Ligandability

Cysteine 225 of TNF receptor-associated factor 4

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 243 of TNF receptor-associated factor 4

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 TNF receptor-associated factor 4 between cysteines 198 and 214.

Details

Redox score ?
82
PDB code
2eod
Structure name
solution structure of traf-type zinc finger domains (190- 248) from human tnf receptor-associated factor 4
Structure deposition date
2007-03-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
9
% buried
0
Peptide accession
Q9BUZ4
Residue number A
198
Residue number B
214
Peptide name
TNF receptor-associated factor 4

Ligandability

Cysteine 198 of TNF receptor-associated factor 4

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 214 of TNF receptor-associated factor 4

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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