ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Cd1d1 protein

Intramolecular
Cysteine 95 and cysteine 150
Cysteine 30 and cysteine 30
Cysteine 30 and cysteine 150
A redox-regulated disulphide may form within Cd1d1 protein between cysteines 95 and 150 (206 and 261 respectively in this structure).

Details

Redox score ?
80
PDB code
4mng
Structure name
structure of the dp10
Structure deposition date
2013-09-10
Thiol separation (Å)
2
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q7TMK5
Residue number A
95
Residue number B
150
Peptide name
Cd1d1 protein

Ligandability

Cysteine 95 of Cd1d1 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 150 of Cd1d1 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 Cd1d1 protein between cysteines 30 and 30 (12 and 166 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
4mng
Structure name
structure of the dp10
Structure deposition date
2013-09-10
Thiol separation (Å)
6
Half-sphere exposure sum ?
78
Minimum pKa ?
12
% buried
nan
Peptide accession
Q7TMK5
Residue number A
30
Residue number B
30
Peptide name
Cd1d1 protein

Ligandability

Cysteine 30 of Cd1d1 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 30 of Cd1d1 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.

Uncertain whether structure cysteine 166 has been assigned to correct residue.
A redox-regulated disulphide may form within Cd1d1 protein between cysteines 30 and 150 (12 and 102 respectively in this structure).

Details

Redox score ?
nan
PDB code
4mq7
Structure name
structure of human cd1d-sulfatide
Structure deposition date
2013-09-15
Thiol separation (Å)
8
Half-sphere exposure sum ?
70
Minimum pKa ?
12
% buried
nan
Peptide accession
Q7TMK5
Residue number A
30
Residue number B
150
Peptide name
Cd1d1 protein

Ligandability

Cysteine 30 of Cd1d1 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 150 of Cd1d1 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.

Uncertain whether structure cysteine 102 has been assigned to correct residue.
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