ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

ADP-ribosylation factor GTPase-activating protein 2

Intramolecular
Cysteine 26 and cysteine 49
Cysteine 29 and cysteine 49
Cysteine 46 and cysteine 49
Cysteine 29 and cysteine 46
Cysteine 26 and cysteine 29
Cysteine 26 and cysteine 46
A redox-regulated disulphide may form within ADP-ribosylation factor GTPase-activating protein 2 between cysteines 26 and 49.

Details

Redox score ?
74
PDB code
2p57
Structure name
gap domain of znf289, an id1-regulated zinc finger protein
Structure deposition date
2007-03-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8N6H7
Residue number A
26
Residue number B
49
Peptide name
ADP-ribosylation factor GTPase-activating protein 2

Ligandability

Cysteine 26 of ADP-ribosylation factor GTPase-activating protein 2

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 49 of ADP-ribosylation factor GTPase-activating protein 2

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 GTPase-activating protein 2 between cysteines 29 and 49.

Details

Redox score ?
72
PDB code
2p57
Structure name
gap domain of znf289, an id1-regulated zinc finger protein
Structure deposition date
2007-03-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8N6H7
Residue number A
29
Residue number B
49
Peptide name
ADP-ribosylation factor GTPase-activating protein 2

Ligandability

Cysteine 29 of ADP-ribosylation factor GTPase-activating protein 2

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 49 of ADP-ribosylation factor GTPase-activating protein 2

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 GTPase-activating protein 2 between cysteines 46 and 49.

Details

Redox score ?
72
PDB code
2p57
Structure name
gap domain of znf289, an id1-regulated zinc finger protein
Structure deposition date
2007-03-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8N6H7
Residue number A
46
Residue number B
49
Peptide name
ADP-ribosylation factor GTPase-activating protein 2

Ligandability

Cysteine 46 of ADP-ribosylation factor GTPase-activating protein 2

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 49 of ADP-ribosylation factor GTPase-activating protein 2

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 GTPase-activating protein 2 between cysteines 29 and 46.

Details

Redox score ?
72
PDB code
2p57
Structure name
gap domain of znf289, an id1-regulated zinc finger protein
Structure deposition date
2007-03-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8N6H7
Residue number A
29
Residue number B
46
Peptide name
ADP-ribosylation factor GTPase-activating protein 2

Ligandability

Cysteine 29 of ADP-ribosylation factor GTPase-activating protein 2

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 46 of ADP-ribosylation factor GTPase-activating protein 2

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 GTPase-activating protein 2 between cysteines 26 and 29.

Details

Redox score ?
71
PDB code
2p57
Structure name
gap domain of znf289, an id1-regulated zinc finger protein
Structure deposition date
2007-03-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8N6H7
Residue number A
26
Residue number B
29
Peptide name
ADP-ribosylation factor GTPase-activating protein 2

Ligandability

Cysteine 26 of ADP-ribosylation factor GTPase-activating protein 2

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 29 of ADP-ribosylation factor GTPase-activating protein 2

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 GTPase-activating protein 2 between cysteines 26 and 46.

Details

Redox score ?
70
PDB code
2p57
Structure name
gap domain of znf289, an id1-regulated zinc finger protein
Structure deposition date
2007-03-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8N6H7
Residue number A
26
Residue number B
46
Peptide name
ADP-ribosylation factor GTPase-activating protein 2

Ligandability

Cysteine 26 of ADP-ribosylation factor GTPase-activating protein 2

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 46 of ADP-ribosylation factor GTPase-activating protein 2

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.

If this tool was useful for finding a disulphide, please cite: