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 282
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 ?
75
PDB code
7k80
Structure name
kir3dl1*001 in complex with hla-a*24:02 presenting the rypltfgw peptide
Structure deposition date
2020-09-24
Thiol separation (Å)
3
Half-sphere exposure sum ?
77
Minimum pKa ?
8
% buried
93
Peptide accession
A0A411J078
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 ?
74
PDB code
7jyu
Structure name
crystal structure of hla-a*2402 in complex with iyfspirvtf, an 10-mer epitope from influenza b virus
Structure deposition date
2020-09-01
Thiol separation (Å)
3
Half-sphere exposure sum ?
83
Minimum pKa ?
8
% buried
80
Peptide accession
A0A411J078
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 282 (227 and 282 respectively in this structure).

Details

Redox score ?
nan
PDB code
7srk
Structure name
single chain trimer hla-a*24:02 (y108c, a163c) with 8mer peptide yppvpetf
Structure deposition date
2021-11-08
Thiol separation (Å)
2
Half-sphere exposure sum ?
45
Minimum pKa ?
nan
% buried
nan
Peptide accession
A0A411J078
Residue number A
125
Residue number B
282
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 282 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 227 has been assigned to correct residue.
Cysteine 282 in protein B could not be asigned to a Uniprot residue.
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