ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Ig-like domain-containing protein

Intermolecular
Cysteine 42 of Ig-like domain-containing protein and cysteine 168
Intramolecular
Cysteine 161 and cysteine 109
Cysteine 161 and cysteine 222
A redox-regulated disulphide may form between two units of Ig-like domain-containing protein at cysteines 42 and 168 (166 and 168 respectively in this structure).

Details

Redox score ?
nan
PDB code
5m00
Structure name
crystal structure of murine p14 tcr complex with h-2db and y4a, modified gp33 peptide from lcmv
Structure deposition date
2016-10-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide A name
Ig-like domain-containing protein
Peptide B name
Ig-like domain-containing protein
Peptide A accession
Q6PIR9
Peptide B accession
Q7TND8
Peptide A residue number
42
Peptide B residue number
168

Ligandability

Cysteine 42 of Ig-like domain-containing 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 168 of Ig-like domain-containing 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 168 in protein B could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within Ig-like domain-containing protein between cysteines 161 and 109 (21 and 89 respectively in this structure).

Details

Redox score ?
81
PDB code
5m00
Structure name
crystal structure of murine p14 tcr complex with h-2db and y4a, modified gp33 peptide from lcmv
Structure deposition date
2016-10-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
89
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q7TND8
Residue number A
161
Residue number B
109
Peptide name
Ig-like domain-containing protein

Ligandability

Cysteine 161 of Ig-like domain-containing 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 109 of Ig-like domain-containing 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.

A redox-regulated disulphide may form within Ig-like domain-containing protein between cysteines 161 and 222 (142 and 203 respectively in this structure).

Details

Redox score ?
78
PDB code
5m00
Structure name
crystal structure of murine p14 tcr complex with h-2db and y4a, modified gp33 peptide from lcmv
Structure deposition date
2016-10-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
90
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q7TND8
Residue number A
161
Residue number B
222
Peptide name
Ig-like domain-containing protein

Ligandability

Cysteine 161 of Ig-like domain-containing 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 222 of Ig-like domain-containing 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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