ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

TRA@ protein

Intermolecular
Cysteine 176 of Human nkt tcr beta chain and cysteine 43
Cysteine 176 of Human nkt tcr beta chain and cysteine 167
Intramolecular
Cysteine 8 and cysteine 8
Cysteine 111 and cysteine 111
Cysteine 43 and cysteine 111
Cysteine 163 and cysteine 214
A redox-regulated disulphide may form between cysteine 176 of Human nkt tcr beta chain and cysteine 43 of TRA@ protein (173 and 167 respectively in this structure).

Details

Redox score ?
80
PDB code
4mnh
Structure name
structure of the dp10
Structure deposition date
2013-09-10
Thiol separation (Å)
2
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide A name
Human nkt tcr beta chain
Peptide B name
TRA@ protein
Peptide A accession
K7N5M4
Peptide B accession
Q6PJ56
Peptide A residue number
176
Peptide B residue number
43

Ligandability

Cysteine 176 of Human nkt tcr beta chain

Cysteine 43 of TRA@ protein

A redox-regulated disulphide may form between cysteine 176 of Human nkt tcr beta chain and cysteine 167 of TRA@ protein (173 and 167 respectively in this structure).

Details

Redox score ?
79
PDB code
4mnh
Structure name
structure of the dp10
Structure deposition date
2013-09-10
Thiol separation (Å)
2
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide A name
Human nkt tcr beta chain
Peptide B name
TRA@ protein
Peptide A accession
K7N5M4
Peptide B accession
Q6PJ56
Peptide A residue number
176
Peptide B residue number
167

Ligandability

Cysteine 176 of Human nkt tcr beta chain

Cysteine 167 of TRA@ protein

Cysteine 167 in protein B could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within TRA@ protein between cysteines 8 and 8 (142 and 192 respectively in this structure).

Details

Redox score ?
82
PDB code
4mnh
Structure name
structure of the dp10
Structure deposition date
2013-09-10
Thiol separation (Å)
2
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6PJ56
Residue number A
8
Residue number B
8
Peptide name
TRA@ protein

Ligandability

Cysteine 8 of TRA@ protein

Cysteine 8 of TRA@ protein

A redox-regulated disulphide may form within TRA@ protein between cysteines 111 and 111 (162 and 234 respectively in this structure).

Details

Redox score ?
82
PDB code
4mng
Structure name
structure of the dp10
Structure deposition date
2013-09-10
Thiol separation (Å)
2
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6PJ56
Residue number A
111
Residue number B
111
Peptide name
TRA@ protein

Ligandability

Cysteine 111 of TRA@ protein

Cysteine 111 of TRA@ protein

A redox-regulated disulphide may form within TRA@ protein between cysteines 43 and 111 (23 and 91 respectively in this structure).

Details

Redox score ?
81
PDB code
4mnh
Structure name
structure of the dp10
Structure deposition date
2013-09-10
Thiol separation (Å)
2
Half-sphere exposure sum ?
84
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6PJ56
Residue number A
43
Residue number B
111
Peptide name
TRA@ protein

Ligandability

Cysteine 43 of TRA@ protein

Cysteine 111 of TRA@ protein

A redox-regulated disulphide may form within TRA@ protein between cysteines 163 and 214 (136 and 187 respectively in this structure).

Details

Redox score ?
80
PDB code
6d7g
Structure name
structure of 5f3 tcr in complex with hla-a2/mart-1
Structure deposition date
2018-04-24
Thiol separation (Å)
2
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6PJ56
Residue number A
163
Residue number B
214
Peptide name
TRA@ protein

Ligandability

Cysteine 163 of TRA@ protein

Cysteine 214 of TRA@ protein

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