ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Igh protein

Intramolecular
Cysteine 383 and cysteine 441
Cysteine 277 and cysteine 337
Cysteine 41 and cysteine 115
Cysteine 166 and cysteine 221
A redox-regulated disulphide may form within Igh protein between cysteines 383 and 441 (370 and 428 respectively in this structure).

Details

Redox score ?
81
PDB code
3hkf
Structure name
murine unglycosylated igg fc fragment
Structure deposition date
2009-05-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q99LC4
Residue number A
383
Residue number B
441
Peptide name
Igh protein

Ligandability

Cysteine 383 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 441 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 277 and 337 (264 and 324 respectively in this structure).

Details

Redox score ?
81
PDB code
3hkf
Structure name
murine unglycosylated igg fc fragment
Structure deposition date
2009-05-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q99LC4
Residue number A
277
Residue number B
337
Peptide name
Igh protein

Ligandability

Cysteine 277 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 337 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 41 and 115 (22 and 92 respectively in this structure).

Details

Redox score ?
80
PDB code
2ntf
Structure name
crystal structure of a quorum-quenching antibody in complex with an n- acyl-l-homoserine lactone analog
Structure deposition date
2006-11-07
Thiol separation (Å)
2
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q99LC4
Residue number A
41
Residue number B
115
Peptide name
Igh protein

Ligandability

Cysteine 41 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 115 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 166 and 221 (140 and 195 respectively in this structure).

Details

Redox score ?
78
PDB code
6c5k
Structure name
s25-23 fab in complex with chlamydiaceae lps (crystal form 2)
Structure deposition date
2018-01-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
88
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q99LC4
Residue number A
166
Residue number B
221
Peptide name
Igh protein

Ligandability

Cysteine 166 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 221 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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