ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Glycolipid transfer protein

Intramolecular
Cysteine 112 and cysteine 176
Cysteine 36 and cysteine 176
A redox-regulated disulphide may form within Glycolipid transfer protein between cysteines 112 and 176. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
2eum
Structure name
crystal structure of human glycolipid transfer protein complexed with 8:0 lactosylceramide
Structure deposition date
2005-10-28
Thiol separation (Å)
8
Half-sphere exposure sum ?
54
Minimum pKa ?
10
% buried
46
Peptide accession
Q9NZD2
Residue number A
112
Residue number B
176
Peptide name
Glycolipid transfer protein

Ligandability

Cysteine 112 of Glycolipid transfer protein

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 176 of Glycolipid transfer protein

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 Glycolipid transfer protein between cysteines 36 and 176. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
2evs
Structure name
crystal structure of human glycolipid transfer protein complexed with n-hexyl-beta-d-glucoside
Structure deposition date
2005-10-31
Thiol separation (Å)
9
Half-sphere exposure sum ?
47
Minimum pKa ?
10
% buried
28
Peptide accession
Q9NZD2
Residue number A
36
Residue number B
176
Peptide name
Glycolipid transfer protein

Ligandability

Cysteine 36 of Glycolipid transfer protein

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 176 of Glycolipid transfer protein

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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