ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Antigen-presenting glycoprotein CD1d

Intramolecular
Cysteine 120 and cysteine 184
Cysteine 224 and cysteine 279
Cysteine 30 and cysteine 120
Cysteine 30 and cysteine 184
A redox-regulated disulphide may form within Antigen-presenting glycoprotein CD1d between cysteines 120 and 184 (102 and 166 respectively in this structure).

Details

Redox score ?
78
PDB code
4ww2
Structure name
crystal structure of human tcr alpha chain-trav21-traj8, beta chain- trbv7-8, antigen-presenting glycoprotein cd1d, and beta-2- microglobulin
Structure deposition date
2014-11-10
Thiol separation (Å)
3
Half-sphere exposure sum ?
70
Minimum pKa ?
8
% buried
82
Peptide accession
P15813
Residue number A
120
Residue number B
184
Peptide name
Antigen-presenting glycoprotein CD1d

Ligandability

Cysteine 120 of Antigen-presenting glycoprotein CD1d

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 184 of Antigen-presenting glycoprotein CD1d

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 Antigen-presenting glycoprotein CD1d between cysteines 224 and 279 (206 and 261 respectively in this structure).

Details

Redox score ?
74
PDB code
4wwk
Structure name
crystal structure of human tcr alpha chain-trav12-3, beta chain-trbv6- 5, antigen-presenting molecule cd1d, and beta-2-microglobulin
Structure deposition date
2014-11-11
Thiol separation (Å)
3
Half-sphere exposure sum ?
81
Minimum pKa ?
8
% buried
75
Peptide accession
P15813
Residue number A
224
Residue number B
279
Peptide name
Antigen-presenting glycoprotein CD1d

Ligandability

Cysteine 224 of Antigen-presenting glycoprotein CD1d

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 279 of Antigen-presenting glycoprotein CD1d

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 Antigen-presenting glycoprotein CD1d between cysteines 30 and 120 (12 and 102 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
3sdx
Structure name
crystal structure of human autoreactive-valpha24 nkt tcr in complex with cd1d-beta-galactosylceramide
Structure deposition date
2011-06-09
Thiol separation (Å)
8
Half-sphere exposure sum ?
71
Minimum pKa ?
12
% buried
nan
Peptide accession
P15813
Residue number A
30
Residue number B
120
Peptide name
Antigen-presenting glycoprotein CD1d

Ligandability

Cysteine 30 of Antigen-presenting glycoprotein CD1d

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 120 of Antigen-presenting glycoprotein CD1d

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 Antigen-presenting glycoprotein CD1d between cysteines 30 and 184 (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 ?
34
PDB code
6v80
Structure name
crystal structure of human cd1d presenting alpha-galactosylceramide in complex with nkt12 tcr and vhh nanobody 1d12
Structure deposition date
2019-12-10
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
12
% buried
nan
Peptide accession
P15813
Residue number A
30
Residue number B
184
Peptide name
Antigen-presenting glycoprotein CD1d

Ligandability

Cysteine 30 of Antigen-presenting glycoprotein CD1d

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 184 of Antigen-presenting glycoprotein CD1d

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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