ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Uncharacterized protein DKFZp686C11235

Intramolecular
Cysteine 239 and cysteine 41
Cysteine 287 and cysteine 347
Cysteine 393 and cysteine 451
A redox-regulated disulphide may form within Uncharacterized protein DKFZp686C11235 between cysteines 239 and 41 (239 and 609 respectively in this structure).

Details

Redox score ?
92
PDB code
6p6d
Structure name
human igg1 fc fragment, c239 insertion mutant
Structure deposition date
2019-06-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6MZV7
Residue number A
239
Residue number B
41
Peptide name
Uncharacterized protein DKFZp686C11235

Ligandability

Cysteine 239 of Uncharacterized protein DKFZp686C11235

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 41 of Uncharacterized protein DKFZp686C11235

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 239 in protein A could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within Uncharacterized protein DKFZp686C11235 between cysteines 287 and 347 (261 and 321 respectively in this structure).

Details

Redox score ?
80
PDB code
5nsg
Structure name
fc dede homodimer variant
Structure deposition date
2017-04-26
Thiol separation (Å)
2
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6MZV7
Residue number A
287
Residue number B
347
Peptide name
Uncharacterized protein DKFZp686C11235

Ligandability

Cysteine 287 of Uncharacterized protein DKFZp686C11235

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 347 of Uncharacterized protein DKFZp686C11235

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 Uncharacterized protein DKFZp686C11235 between cysteines 393 and 451 (367 and 425 respectively in this structure).

Details

Redox score ?
80
PDB code
5vme
Structure name
crystal structure of human igg1 fc k248e, t437r mutant
Structure deposition date
2017-04-27
Thiol separation (Å)
2
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6MZV7
Residue number A
393
Residue number B
451
Peptide name
Uncharacterized protein DKFZp686C11235

Ligandability

Cysteine 393 of Uncharacterized protein DKFZp686C11235

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 451 of Uncharacterized protein DKFZp686C11235

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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