ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Ganglioside GM2 activator

Intramolecular
Cysteine 125 and cysteine 136
Cysteine 112 and cysteine 138
Cysteine 99 and cysteine 106
Cysteine 39 and cysteine 183
Cysteine 136 and cysteine 138
A redox-regulated disulphide may form within Ganglioside GM2 activator between cysteines 125 and 136 (94 and 105 respectively in this structure).

Details

Redox score ?
87
PDB code
1pub
Structure name
gm2-activator protein crystal structure
Structure deposition date
2003-06-24
Thiol separation (Å)
2
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17900
Residue number A
125
Residue number B
136
Peptide name
Ganglioside GM2 activator

Ligandability

Cysteine 125 of Ganglioside GM2 activator

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 136 of Ganglioside GM2 activator

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 Ganglioside GM2 activator between cysteines 112 and 138 (83 and 109 respectively in this structure).

Details

Redox score ?
84
PDB code
1pu5
Structure name
gm2-activator protein crystal structure
Structure deposition date
2003-06-24
Thiol separation (Å)
2
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17900
Residue number A
112
Residue number B
138
Peptide name
Ganglioside GM2 activator

Ligandability

Cysteine 112 of Ganglioside GM2 activator

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 138 of Ganglioside GM2 activator

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 Ganglioside GM2 activator between cysteines 99 and 106 (70 and 77 respectively in this structure).

Details

Redox score ?
84
PDB code
1tjj
Structure name
human gm2 activator protein paf complex
Structure deposition date
2004-06-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17900
Residue number A
99
Residue number B
106
Peptide name
Ganglioside GM2 activator

Ligandability

Cysteine 99 of Ganglioside GM2 activator

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 106 of Ganglioside GM2 activator

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 Ganglioside GM2 activator between cysteines 39 and 183 (8 and 152 respectively in this structure).

Details

Redox score ?
82
PDB code
1pub
Structure name
gm2-activator protein crystal structure
Structure deposition date
2003-06-24
Thiol separation (Å)
2
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17900
Residue number A
39
Residue number B
183
Peptide name
Ganglioside GM2 activator

Ligandability

Cysteine 39 of Ganglioside GM2 activator

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 183 of Ganglioside GM2 activator

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 Ganglioside GM2 activator between cysteines 136 and 138 (107 and 109 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
2ag4
Structure name
crystal structure analysis of gm2-activator protein complexed with phosphatidylcholine
Structure deposition date
2005-07-26
Thiol separation (Å)
10
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17900
Residue number A
136
Residue number B
138
Peptide name
Ganglioside GM2 activator

Ligandability

Cysteine 136 of Ganglioside GM2 activator

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 138 of Ganglioside GM2 activator

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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