ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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ADP-ribosylation factor-binding protein GGA3

Intramolecular
Cysteine 33 and cysteine 76
Cysteine 33 and cysteine 72
Cysteine 72 and cysteine 76
A redox-regulated disulphide may form within ADP-ribosylation factor-binding protein GGA3 between cysteines 33 and 76.

Details

Redox score ?
74
PDB code
1lf8
Structure name
complex of gga3-vhs domain and ci-mpr c-terminal phosphopeptide
Structure deposition date
2002-04-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
77
Minimum pKa ?
6
% buried
98
Peptide accession
Q9NZ52
Residue number A
33
Residue number B
76
Peptide name
ADP-ribosylation factor-binding protein GGA3

Ligandability

Cysteine 33 of ADP-ribosylation factor-binding protein GGA3

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 76 of ADP-ribosylation factor-binding protein GGA3

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-binding protein GGA3 between cysteines 33 and 72. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
59
PDB code
1lf8
Structure name
complex of gga3-vhs domain and ci-mpr c-terminal phosphopeptide
Structure deposition date
2002-04-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
77
Minimum pKa ?
14
% buried
100
Peptide accession
Q9NZ52
Residue number A
33
Residue number B
72
Peptide name
ADP-ribosylation factor-binding protein GGA3

Ligandability

Cysteine 33 of ADP-ribosylation factor-binding protein GGA3

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 72 of ADP-ribosylation factor-binding protein GGA3

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-binding protein GGA3 between cysteines 72 and 76. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
59
PDB code
1lf8
Structure name
complex of gga3-vhs domain and ci-mpr c-terminal phosphopeptide
Structure deposition date
2002-04-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
74
Minimum pKa ?
14
% buried
98
Peptide accession
Q9NZ52
Residue number A
72
Residue number B
76
Peptide name
ADP-ribosylation factor-binding protein GGA3

Ligandability

Cysteine 72 of ADP-ribosylation factor-binding protein GGA3

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 76 of ADP-ribosylation factor-binding protein GGA3

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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