ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Ighg protein

Intermolecular
Cysteine 155 and cysteine 234 of MAb 6H10 light chain
Intramolecular
Cysteine 396 and cysteine 115
Cysteine 41 and cysteine 115
Cysteine 167 and cysteine 222
A redox-regulated disulphide may form between cysteine 155 of Ighg protein and cysteine 234 of MAb 6H10 light chain (139 and 214 respectively in this structure).

Details

Redox score ?
90
PDB code
6u2f
Structure name
pcsk9-fab 7g7 complex bound to cis-1-amino-4-phenylcyclohexaneacyl- wnlk(hr)igllr - nh2
Structure deposition date
2019-08-19
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide A name
Ighg protein
Peptide B name
MAb 6H10 light chain
Peptide A accession
Q569X1
Peptide B accession
A0A0U5BC76
Peptide A residue number
155
Peptide B residue number
234

Ligandability

Cysteine 155 of Ighg 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 234 of MAb 6H10 light 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.

A redox-regulated disulphide may form within Ighg protein between cysteines 396 and 115 (22 and 95 respectively in this structure).

Details

Redox score ?
81
PDB code
5vxr
Structure name
the antigen-binding fragment of mab24 in complex with a peptide from hepatitis c virus e2 epitope i (412-423)
Structure deposition date
2017-05-24
Thiol separation (Å)
2
Half-sphere exposure sum ?
84
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q569X1
Residue number A
396
Residue number B
115
Peptide name
Ighg protein

Ligandability

Cysteine 396 of Ighg 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 115 of Ighg 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 Ighg protein between cysteines 41 and 115 (22 and 96 respectively in this structure).

Details

Redox score ?
79
PDB code
5ikc
Structure name
x-ray structure of the n-terminal domain of human doublecortin in complex with fab
Structure deposition date
2016-03-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
85
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q569X1
Residue number A
41
Residue number B
115
Peptide name
Ighg protein

Ligandability

Cysteine 41 of Ighg 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 115 of Ighg 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 Ighg protein between cysteines 167 and 222 (142 and 197 respectively in this structure).

Details

Redox score ?
79
PDB code
5ikc
Structure name
x-ray structure of the n-terminal domain of human doublecortin in complex with fab
Structure deposition date
2016-03-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
89
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q569X1
Residue number A
167
Residue number B
222
Peptide name
Ighg protein

Ligandability

Cysteine 167 of Ighg 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 Ighg 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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