ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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TRB protein

Intermolecular
Cysteine 161 of T-cell receptor, sp3.4 alpha chain and cysteine 171
Intramolecular
Cysteine 75 and cysteine 19
Cysteine 75 and cysteine 140
A redox-regulated disulphide may form between cysteine 161 of T-cell receptor, sp3.4 alpha chain and cysteine 171 of TRB protein (158 and 171 respectively in this structure).

Details

Redox score ?
79
PDB code
5nht
Structure name
human 199
Structure deposition date
2017-03-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide A name
T-cell receptor, sp3
Peptide B name
TRB protein
Peptide A accession
K7N5N2
Peptide B accession
A0A0C4ZKA8
Peptide A residue number
161
Peptide B residue number
171

Ligandability

Cysteine 161 of T-cell receptor, sp3.4 alpha chain

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 171 of TRB protein

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 171 in protein B could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within TRB protein between cysteines 75 and 19 (23 and 91 respectively in this structure).

Details

Redox score ?
81
PDB code
5nht
Structure name
human 199
Structure deposition date
2017-03-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
84
Minimum pKa ?
nan
% buried
nan
Peptide accession
A0A0C4ZKA8
Residue number A
75
Residue number B
19
Peptide name
TRB protein

Ligandability

Cysteine 75 of TRB protein

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 19 of TRB protein

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.

Uncertain whether structure cysteine 23 has been assigned to correct residue.
A redox-regulated disulphide may form within TRB protein between cysteines 75 and 140 (145 and 210 respectively in this structure).

Details

Redox score ?
79
PDB code
5nqk
Structure name
human 199
Structure deposition date
2017-04-20
Thiol separation (Å)
2
Half-sphere exposure sum ?
92
Minimum pKa ?
nan
% buried
nan
Peptide accession
A0A0C4ZKA8
Residue number A
75
Residue number B
140
Peptide name
TRB protein

Ligandability

Cysteine 75 of TRB protein

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 140 of TRB protein

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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