ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

H-2D cell surface glycoprotein

Intramolecular
Cysteine 202 and cysteine 258
Cysteine 100 and cysteine 163
A redox-regulated disulphide may form within H-2D cell surface glycoprotein between cysteines 202 and 258 (203 and 259 respectively in this structure).

Details

Redox score ?
82
PDB code
6h6h
Structure name
crystal structures of the murine class i major histocompatibility complex h-2dbm13 in complex with adenovirus-derived peptide ad10
Structure deposition date
2018-07-27
Thiol separation (Å)
2
Half-sphere exposure sum ?
84
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q31167
Residue number A
202
Residue number B
258
Peptide name
H-2D cell surface glycoprotein

Ligandability

Cysteine 202 of H-2D cell surface glycoprotein

Cysteine 258 of H-2D cell surface glycoprotein

A redox-regulated disulphide may form within H-2D cell surface glycoprotein between cysteines 100 and 163 (101 and 164 respectively in this structure).

Details

Redox score ?
82
PDB code
6h6h
Structure name
crystal structures of the murine class i major histocompatibility complex h-2dbm13 in complex with adenovirus-derived peptide ad10
Structure deposition date
2018-07-27
Thiol separation (Å)
2
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q31167
Residue number A
100
Residue number B
163
Peptide name
H-2D cell surface glycoprotein

Ligandability

Cysteine 100 of H-2D cell surface glycoprotein

Cysteine 163 of H-2D cell surface glycoprotein

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