ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Uncharacterized protein DKFZp686L19235

Intermolecular
Cysteine 306 and cysteine 306
Cysteine 249 and cysteine 249
Cysteine 308 and cysteine 249
Cysteine 308 and cysteine 308
Cysteine 249 and cysteine 306
Intramolecular
Cysteine 273 and cysteine 330
Cysteine 376 and cysteine 439
Cysteine 306 and cysteine 308
A redox-regulated disulphide may form between two units of Uncharacterized protein DKFZp686L19235 at cysteines 306 and 306 (299 and 299 respectively in this structure).

Details

Redox score ?
85
PDB code
7ttz
Structure name
heterodimeric iga fc in complex with staphylococcus aureus protein ssl7
Structure deposition date
2022-02-02
Thiol separation (Å)
2
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide A name
Uncharacterized protein DKFZp686L19235
Peptide B name
Uncharacterized protein DKFZp686L19235
Peptide A accession
Q6MZV6
Peptide B accession
Q6MZV6
Peptide A residue number
306
Peptide B residue number
306

Ligandability

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 two units of Uncharacterized protein DKFZp686L19235 at cysteines 249 and 249 (242 and 242 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
7ttz
Structure name
heterodimeric iga fc in complex with staphylococcus aureus protein ssl7
Structure deposition date
2022-02-02
Thiol separation (Å)
9
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide A name
Uncharacterized protein DKFZp686L19235
Peptide B name
Uncharacterized protein DKFZp686L19235
Peptide A accession
Q6MZV6
Peptide B accession
Q6MZV6
Peptide A residue number
249
Peptide B residue number
249

Ligandability

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 two units of Uncharacterized protein DKFZp686L19235 at cysteines 308 and 249 (301 and 242 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
7ttz
Structure name
heterodimeric iga fc in complex with staphylococcus aureus protein ssl7
Structure deposition date
2022-02-02
Thiol separation (Å)
9
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide A name
Uncharacterized protein DKFZp686L19235
Peptide B name
Uncharacterized protein DKFZp686L19235
Peptide A accession
Q6MZV6
Peptide B accession
Q6MZV6
Peptide A residue number
308
Peptide B residue number
249

Ligandability

Cysteine 308 of Uncharacterized protein DKFZp686L19235

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 249 of Uncharacterized protein DKFZp686L19235

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 two units of Uncharacterized protein DKFZp686L19235 at cysteines 308 and 308 (301 and 301 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
7ttz
Structure name
heterodimeric iga fc in complex with staphylococcus aureus protein ssl7
Structure deposition date
2022-02-02
Thiol separation (Å)
8
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide A name
Uncharacterized protein DKFZp686L19235
Peptide B name
Uncharacterized protein DKFZp686L19235
Peptide A accession
Q6MZV6
Peptide B accession
Q6MZV6
Peptide A residue number
308
Peptide B residue number
308

Ligandability

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 two units of Uncharacterized protein DKFZp686L19235 at cysteines 249 and 306 (242 and 299 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
7ttz
Structure name
heterodimeric iga fc in complex with staphylococcus aureus protein ssl7
Structure deposition date
2022-02-02
Thiol separation (Å)
9
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide A name
Uncharacterized protein DKFZp686L19235
Peptide B name
Uncharacterized protein DKFZp686L19235
Peptide A accession
Q6MZV6
Peptide B accession
Q6MZV6
Peptide A residue number
249
Peptide B residue number
306

Ligandability

Cysteine 249 of Uncharacterized protein DKFZp686L19235

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 306 of Uncharacterized protein DKFZp686L19235

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 DKFZp686L19235 between cysteines 273 and 330 (266 and 323 respectively in this structure).

Details

Redox score ?
84
PDB code
7ttz
Structure name
heterodimeric iga fc in complex with staphylococcus aureus protein ssl7
Structure deposition date
2022-02-02
Thiol separation (Å)
2
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6MZV6
Residue number A
273
Residue number B
330
Peptide name
Uncharacterized protein DKFZp686L19235

Ligandability

Cysteine 273 of Uncharacterized protein DKFZp686L19235

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 330 of Uncharacterized protein DKFZp686L19235

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 DKFZp686L19235 between cysteines 376 and 439 (369 and 432 respectively in this structure).

Details

Redox score ?
78
PDB code
7ttz
Structure name
heterodimeric iga fc in complex with staphylococcus aureus protein ssl7
Structure deposition date
2022-02-02
Thiol separation (Å)
2
Half-sphere exposure sum ?
89
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6MZV6
Residue number A
376
Residue number B
439
Peptide name
Uncharacterized protein DKFZp686L19235

Ligandability

Cysteine 376 of Uncharacterized protein DKFZp686L19235

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 439 of Uncharacterized protein DKFZp686L19235

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 DKFZp686L19235 between cysteines 306 and 308 (299 and 301 respectively in this structure).

Details

Redox score ?
75
PDB code
7ttz
Structure name
heterodimeric iga fc in complex with staphylococcus aureus protein ssl7
Structure deposition date
2022-02-02
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6MZV6
Residue number A
306
Residue number B
308
Peptide name
Uncharacterized protein DKFZp686L19235

Ligandability

Cysteine 306 of Uncharacterized protein DKFZp686L19235

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 308 of Uncharacterized protein DKFZp686L19235

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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