ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Igh protein

Intramolecular
Cysteine 291 and cysteine 351
Cysteine 397 and cysteine 455
A redox-regulated disulphide may form within Igh protein between cysteines 291 and 351 (261 and 321 respectively in this structure).

Details

Redox score ?
82
PDB code
6bhq
Structure name
mouse immunoglobulin g 2c fc fragment with complex-type glycan
Structure deposition date
2017-10-31
Thiol separation (Å)
2
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q58E56
Residue number A
291
Residue number B
351
Peptide name
Igh protein

Ligandability

Cysteine 291 of Igh 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 351 of Igh 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 Igh protein between cysteines 397 and 455 (367 and 425 respectively in this structure).

Details

Redox score ?
81
PDB code
6bhy
Structure name
mouse immunoglobulin g 2c fc fragment with single glcnac
Structure deposition date
2017-10-31
Thiol separation (Å)
2
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q58E56
Residue number A
397
Residue number B
455
Peptide name
Igh protein

Ligandability

Cysteine 397 of Igh 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 455 of Igh 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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