ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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IgG H chain

Intermolecular
Cysteine 109 and cysteine 135 of Pre-glycoprotein polyprotein GP complex
Intramolecular
Cysteine 41 and cysteine 116
Cysteine 172 and cysteine 228
Cysteine 104 and cysteine 109
A redox-regulated disulphide may form between cysteine 109 of IgG H chain and cysteine 135 of Pre-glycoprotein polyprotein GP complex. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
5w1k
Structure name
junv gp1 cr1-10 fab cr1-28 fab complex
Structure deposition date
2017-06-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide A name
IgG H chain
Peptide B name
Pre-glycoprotein polyprotein GP complex
Peptide A accession
S6B2B6
Peptide B accession
P26313
Peptide A residue number
109
Peptide B residue number
135

Ligandability

Cysteine 109 of IgG H 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 135 of Pre-glycoprotein polyprotein GP complex

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 in protein A could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within IgG H chain between cysteines 41 and 116 (22 and 97 respectively in this structure).

Details

Redox score ?
80
PDB code
5w1k
Structure name
junv gp1 cr1-10 fab cr1-28 fab complex
Structure deposition date
2017-06-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
85
Minimum pKa ?
nan
% buried
nan
Peptide accession
S6B2B6
Residue number A
41
Residue number B
116
Peptide name
IgG H chain

Ligandability

Cysteine 41 of IgG H 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 116 of IgG H 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 IgG H chain between cysteines 172 and 228 (153 and 209 respectively in this structure).

Details

Redox score ?
79
PDB code
5w1k
Structure name
junv gp1 cr1-10 fab cr1-28 fab complex
Structure deposition date
2017-06-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
86
Minimum pKa ?
nan
% buried
nan
Peptide accession
S6B2B6
Residue number A
172
Residue number B
228
Peptide name
IgG H chain

Ligandability

Cysteine 172 of IgG H 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 228 of IgG H 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 IgG H chain between cysteines 104 and 109.

Details

Redox score ?
nan
PDB code
5w1k
Structure name
junv gp1 cr1-10 fab cr1-28 fab complex
Structure deposition date
2017-06-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
S6B2B6
Residue number A
104
Residue number B
109
Peptide name
IgG H chain

Ligandability

Cysteine 104 of IgG H 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 109 of IgG H 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 104 in protein A could not be asigned to a Uniprot residue.
Cysteine 109 in protein B could not be asigned to a Uniprot residue.
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