ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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MHC class I heavy chain

Intramolecular
Cysteine 25 and cysteine 280
Cysteine 224 and cysteine 280
Cysteine 122 and cysteine 185
A redox-regulated disulphide may form within MHC class I heavy chain between cysteines 25 and 280 (25 and 80 respectively in this structure).

Details

Redox score ?
94
PDB code
3nwm
Structure name
crystal structure of a single chain construct composed of mhc class i h-2kd, beta-2microglobulin and a peptide which is an autoantigen for type 1 diabetes
Structure deposition date
2010-07-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q5KTQ2
Residue number A
25
Residue number B
280
Peptide name
MHC class I heavy chain

Ligandability

Cysteine 25 of MHC class I heavy chain

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 280 of MHC class I heavy chain

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 25 in protein A could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within MHC class I heavy chain between cysteines 224 and 280 (203 and 259 respectively in this structure).

Details

Redox score ?
94
PDB code
3nwm
Structure name
crystal structure of a single chain construct composed of mhc class i h-2kd, beta-2microglobulin and a peptide which is an autoantigen for type 1 diabetes
Structure deposition date
2010-07-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q5KTQ2
Residue number A
224
Residue number B
280
Peptide name
MHC class I heavy chain

Ligandability

Cysteine 224 of MHC class I heavy chain

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 280 of MHC class I heavy chain

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 heavy chain between cysteines 122 and 185 (101 and 164 respectively in this structure).

Details

Redox score ?
94
PDB code
3nwm
Structure name
crystal structure of a single chain construct composed of mhc class i h-2kd, beta-2microglobulin and a peptide which is an autoantigen for type 1 diabetes
Structure deposition date
2010-07-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q5KTQ2
Residue number A
122
Residue number B
185
Peptide name
MHC class I heavy chain

Ligandability

Cysteine 122 of MHC class I heavy chain

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 185 of MHC class I heavy chain

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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