ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

Ig kappa-b4 chain C region

Intermolecular
Cysteine 103 and cysteine 133 of IgG heavy chain VDJ region
Cysteine 103 and cysteine 134 of IgG heavy chain VDJ region
Intramolecular
Cysteine 26 and cysteine 85
A redox-regulated disulphide may form between cysteine 103 of Ig kappa-b4 chain C region and cysteine 133 of IgG heavy chain VDJ region (237 and 150 respectively in this structure).

Details

Redox score ?
88
PDB code
6did
Structure name
hiv env bg505 sosip with polyclonal fabs from immunized rabbit #3417 post-boost#1
Structure deposition date
2018-05-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide A name
Ig kappa-b4 chain C region
Peptide B name
IgG heavy chain VDJ region
Peptide A accession
P01840
Peptide B accession
A0A1Y1B8B1
Peptide A residue number
103
Peptide B residue number
133

Ligandability

Cysteine 103 of Ig kappa-b4 chain C region

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 133 of IgG heavy chain VDJ region

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 between cysteine 103 of Ig kappa-b4 chain C region and cysteine 134 of IgG heavy chain VDJ region (237 and 151 respectively in this structure).

Details

Redox score ?
61
PDB code
6did
Structure name
hiv env bg505 sosip with polyclonal fabs from immunized rabbit #3417 post-boost#1
Structure deposition date
2018-05-23
Thiol separation (Å)
7
Half-sphere exposure sum ?
nan
Minimum pKa ?
10
% buried
nan
Peptide A name
Ig kappa-b4 chain C region
Peptide B name
IgG heavy chain VDJ region
Peptide A accession
P01840
Peptide B accession
A0A1Y1B8B1
Peptide A residue number
103
Peptide B residue number
134

Ligandability

Cysteine 103 of Ig kappa-b4 chain C region

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 134 of IgG heavy chain VDJ region

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 kappa-b4 chain C region between cysteines 26 and 85 (160 and 219 respectively in this structure).

Details

Redox score ?
77
PDB code
6did
Structure name
hiv env bg505 sosip with polyclonal fabs from immunized rabbit #3417 post-boost#1
Structure deposition date
2018-05-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
87
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01840
Residue number A
26
Residue number B
85
Peptide name
Ig kappa-b4 chain C region

Ligandability

Cysteine 26 of Ig kappa-b4 chain C region

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 85 of Ig kappa-b4 chain C region

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.

If this tool was useful for finding a disulphide, please cite: