ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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MHC class I antigen

Intramolecular
Cysteine 125 and cysteine 188
Cysteine 227 and cysteine 283
Cysteine 125 and cysteine 139
A redox-regulated disulphide may form within MHC class I antigen between cysteines 125 and 188 (101 and 164 respectively in this structure).

Details

Redox score ?
81
PDB code
6tdo
Structure name
crystal structure of the disulfide engineered hla-a0201 molecule in complex with one gm dipeptide in the a pocket
Structure deposition date
2019-11-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
F6IQS1
Residue number A
125
Residue number B
188
Peptide name
MHC class I antigen

Ligandability

Cysteine 125 of MHC class I antigen

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 188 of MHC class I antigen

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 MHC class I antigen between cysteines 227 and 283 (203 and 259 respectively in this structure).

Details

Redox score ?
80
PDB code
6tds
Structure name
crystal structure of the disulfide engineered hla-a0201 molecule without peptide bound after nacl wash
Structure deposition date
2019-11-10
Thiol separation (Å)
2
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
F6IQS1
Residue number A
227
Residue number B
283
Peptide name
MHC class I antigen

Ligandability

Cysteine 227 of MHC class I antigen

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 283 of MHC class I antigen

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 MHC class I antigen between cysteines 125 and 139 (84 and 139 respectively in this structure).

Details

Redox score ?
nan
PDB code
6tdq
Structure name
crystal structure of the disulfide engineered hla-a0201 molecule in complex with one gm dipeptide in the a pocket and one gm dipeptide in the f pocket
Structure deposition date
2019-11-10
Thiol separation (Å)
2
Half-sphere exposure sum ?
42
Minimum pKa ?
nan
% buried
nan
Peptide accession
F6IQS1
Residue number A
125
Residue number B
139
Peptide name
MHC class I antigen

Ligandability

Cysteine 125 of MHC class I antigen

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 139 of MHC class I antigen

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 84 has been assigned to correct residue.
Cysteine 139 in protein B could not be asigned to a Uniprot residue.
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