ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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ADP-ribosylation factor 6

Intramolecular
Cysteine 90 and cysteine 155
Cysteine 292 and cysteine 155
Cysteine 461 and cysteine 464
A redox-regulated disulphide may form within ADP-ribosylation factor 6 between cysteines 90 and 155. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
PDB code
1e0s
Structure name
small g protein arf6-gdp
Structure deposition date
2000-04-06
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
12
% buried
nan
Peptide accession
P62330
Residue number A
90
Residue number B
155
Peptide name
ADP-ribosylation factor 6

Ligandability

Cysteine 90 of ADP-ribosylation factor 6

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 155 of ADP-ribosylation factor 6

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 ADP-ribosylation factor 6 between cysteines 292 and 155 (292 and 342 respectively in this structure).

Details

Redox score ?
nan
PDB code
6bbq
Structure name
model for extended volume of truncated monomeric cytohesin-3 (grp1; amino acids 63-399) e161a arf6 q67l fusion protein
Structure deposition date
2017-10-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
75
Minimum pKa ?
12
% buried
100
Peptide accession
P62330
Residue number A
292
Residue number B
155
Peptide name
ADP-ribosylation factor 6

Ligandability

Cysteine 292 of ADP-ribosylation factor 6

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 155 of ADP-ribosylation factor 6

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 292 in protein A could not be asigned to a Uniprot residue.
Uncertain whether structure cysteine 342 has been assigned to correct residue.
A redox-regulated disulphide may form within ADP-ribosylation factor 6 between cysteines 461 and 464.

Details

Redox score ?
nan
PDB code
3lvr
Structure name
the crystal structure of asap3 in complex with arf6 in transition state soaked with calcium
Structure deposition date
2010-02-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
84
Minimum pKa ?
24
% buried
nan
Peptide accession
P62330
Residue number A
461
Residue number B
464
Peptide name
ADP-ribosylation factor 6

Ligandability

Cysteine 461 of ADP-ribosylation factor 6

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 464 of ADP-ribosylation factor 6

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 461 in protein A could not be asigned to a Uniprot residue.
Cysteine 464 in protein B could not be asigned to a Uniprot residue.
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