ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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IGL@ protein

Intermolecular
Cysteine 234 and cysteine 234
Intramolecular
Cysteine 41 and cysteine 109
Cysteine 157 and cysteine 216
A redox-regulated disulphide may form between two units of IGL@ protein at cysteines 234 and 234 (215 and 215 respectively in this structure).

Details

Redox score ?
87
PDB code
1mcb
Structure name
principles and pitfalls in designing site directed peptide ligands
Structure deposition date
1993-02-25
Thiol separation (Å)
2
Half-sphere exposure sum ?
29
Minimum pKa ?
nan
% buried
nan
Peptide A name
IGL@ protein
Peptide B name
IGL@ protein
Peptide A accession
Q6PIK1
Peptide B accession
Q6PIK1
Peptide A residue number
234
Peptide B residue number
234

Ligandability

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 IGL@ protein between cysteines 41 and 109 (22 and 90 respectively in this structure).

Details

Redox score ?
79
PDB code
1mcb
Structure name
principles and pitfalls in designing site directed peptide ligands
Structure deposition date
1993-02-25
Thiol separation (Å)
2
Half-sphere exposure sum ?
92
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6PIK1
Residue number A
41
Residue number B
109
Peptide name
IGL@ protein

Ligandability

Cysteine 41 of IGL@ 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 IGL@ 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 IGL@ protein between cysteines 157 and 216 (138 and 197 respectively in this structure).

Details

Redox score ?
77
PDB code
1mcb
Structure name
principles and pitfalls in designing site directed peptide ligands
Structure deposition date
1993-02-25
Thiol separation (Å)
2
Half-sphere exposure sum ?
90
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6PIK1
Residue number A
157
Residue number B
216
Peptide name
IGL@ protein

Ligandability

Cysteine 157 of IGL@ 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 216 of IGL@ 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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