ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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If kappa light chain

Intermolecular
Cysteine 219 and cysteine 149 of Igh protein
Cysteine 219 and cysteine 128 of Anti-human Fc gamma receptor III 3G8 gamma heavy chain variable region
Intramolecular
Cysteine 23 and cysteine 93
Cysteine 139 and cysteine 199
A redox-regulated disulphide may form between cysteine 219 of If kappa light chain and cysteine 149 of Igh protein (213 and 128 respectively in this structure).

Details

Redox score ?
70
PDB code
2ipt
Structure name
pfa1 fab fragment
Structure deposition date
2006-10-12
Thiol separation (Å)
6
Half-sphere exposure sum ?
nan
Minimum pKa ?
9
% buried
24
Peptide A name
If kappa light chain
Peptide B name
Igh protein
Peptide A accession
A2NHM3
Peptide B accession
Q6PIP8
Peptide A residue number
219
Peptide B residue number
149

Ligandability

Cysteine 219 of If kappa 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.

Cysteine 149 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 between cysteine 219 of If kappa light chain and cysteine 128 of Anti-human Fc gamma receptor III 3G8 gamma heavy chain variable region (213 and 128 respectively in this structure).

Details

Redox score ?
nan
PDB code
2iqa
Structure name
pfa2 fab fragment, monoclinic apo form
Structure deposition date
2006-10-13
Thiol separation (Å)
7
Half-sphere exposure sum ?
nan
Minimum pKa ?
10
% buried
13
Peptide A name
If kappa light chain
Peptide B name
Anti-human Fc gamma receptor III 3G8 gamma heavy chain variable region
Peptide A accession
A2NHM3
Peptide B accession
Q811U5
Peptide A residue number
219
Peptide B residue number
128

Ligandability

Cysteine 219 of If kappa 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.

Cysteine 128 of Anti-human Fc gamma receptor III 3G8 gamma heavy chain variable 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 128 in protein B could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within If kappa light chain between cysteines 23 and 93 (23 and 88 respectively in this structure).

Details

Redox score ?
81
PDB code
2ipt
Structure name
pfa1 fab fragment
Structure deposition date
2006-10-12
Thiol separation (Å)
2
Half-sphere exposure sum ?
87
Minimum pKa ?
nan
% buried
nan
Peptide accession
A2NHM3
Residue number A
23
Residue number B
93
Peptide name
If kappa light chain

Ligandability

Cysteine 23 of If kappa 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.

Cysteine 93 of If kappa 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 If kappa light chain between cysteines 139 and 199 (134 and 194 respectively in this structure).

Details

Redox score ?
76
PDB code
2dtm
Structure name
thermodynamic and structural analyses of hydrolytic mechanism by catalytic antibodies
Structure deposition date
2006-07-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
92
Minimum pKa ?
nan
% buried
nan
Peptide accession
A2NHM3
Residue number A
139
Residue number B
199
Peptide name
If kappa light chain

Ligandability

Cysteine 139 of If kappa 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.

Cysteine 199 of If kappa 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.

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