ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

HLA class II histocompatibility antigen, DQ beta 1 chain

Intermolecular
Cysteine 11 of HLA class II histocompatibility antigen, DQ alpha 1 chain and cysteine 47
Cysteine 11 of HLA class II histocompatibility antigen, DQ alpha 1 chain and cysteine 111
Intramolecular
Cysteine 47 and cysteine 111
Cysteine 149 and cysteine 205
A redox-regulated disulphide may form between cysteine 11 of HLA class II histocompatibility antigen, DQ alpha 1 chain and cysteine 47 of HLA class II histocompatibility antigen, DQ beta 1 chain (11 and 15 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
1uvq
Structure name
crystal structure of hla-dq0602 in complex with a hypocretin peptide
Structure deposition date
2004-01-22
Thiol separation (Å)
5
Half-sphere exposure sum ?
95
Minimum pKa ?
13
% buried
nan
Peptide A name
HLA class II histocompatibility antigen, DQ alpha 1 chain
Peptide B name
HLA class II histocompatibility antigen, DQ beta 1 chain
Peptide A accession
P01907
Peptide B accession
P03992
Peptide A residue number
11
Peptide B residue number
47

Ligandability

Cysteine 11 of HLA class II histocompatibility antigen, DQ alpha 1 chain

Cysteine 47 of HLA class II histocompatibility antigen, DQ beta 1 chain

Cysteine 11 in protein A could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form between cysteine 11 of HLA class II histocompatibility antigen, DQ alpha 1 chain and cysteine 111 of HLA class II histocompatibility antigen, DQ beta 1 chain (11 and 79 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
1uvq
Structure name
crystal structure of hla-dq0602 in complex with a hypocretin peptide
Structure deposition date
2004-01-22
Thiol separation (Å)
6
Half-sphere exposure sum ?
94
Minimum pKa ?
13
% buried
nan
Peptide A name
HLA class II histocompatibility antigen, DQ alpha 1 chain
Peptide B name
HLA class II histocompatibility antigen, DQ beta 1 chain
Peptide A accession
P01907
Peptide B accession
P03992
Peptide A residue number
11
Peptide B residue number
111

Ligandability

Cysteine 11 of HLA class II histocompatibility antigen, DQ alpha 1 chain

Cysteine 111 of HLA class II histocompatibility antigen, DQ beta 1 chain

Cysteine 11 in protein A could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within HLA class II histocompatibility antigen, DQ beta 1 chain between cysteines 47 and 111 (15 and 79 respectively in this structure).

Details

Redox score ?
80
PDB code
1jk8
Structure name
crystal structure of a human insulin peptide-hla-dq8 complex
Structure deposition date
2001-07-11
Thiol separation (Å)
2
Half-sphere exposure sum ?
83
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01920
Residue number A
47
Residue number B
111
Peptide name
HLA class II histocompatibility antigen, DQ beta 1 chain

Ligandability

Cysteine 47 of HLA class II histocompatibility antigen, DQ beta 1 chain

Cysteine 111 of HLA class II histocompatibility antigen, DQ beta 1 chain

A redox-regulated disulphide may form within HLA class II histocompatibility antigen, DQ beta 1 chain between cysteines 149 and 205 (117 and 173 respectively in this structure).

Details

Redox score ?
80
PDB code
1uvq
Structure name
crystal structure of hla-dq0602 in complex with a hypocretin peptide
Structure deposition date
2004-01-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03992
Residue number A
149
Residue number B
205
Peptide name
HLA class II histocompatibility antigen, DQ beta 1 chain

Ligandability

Cysteine 149 of HLA class II histocompatibility antigen, DQ beta 1 chain

Cysteine 205 of HLA class II histocompatibility antigen, DQ beta 1 chain

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