ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

H-2 class II histocompatibility antigen, A-D alpha chain

Intermolecular
Cysteine 74 and cysteine 107 of Insulin-1
Cysteine 11 and cysteine 47 of HLA class II histocompatibility antigen, DQ beta 1 chain
Cysteine 11 and cysteine 111 of HLA class II histocompatibility antigen, DQ beta 1 chain
Intramolecular
Cysteine 132 and cysteine 188
Cysteine 15 and cysteine 79
A redox-regulated disulphide may form between cysteine 74 of H-2 class II histocompatibility antigen, A-D alpha chain and cysteine 107 of Insulin-1 (74 and 11 respectively in this structure).

Details

Redox score ?
85
PDB code
7qhp
Structure name
structure of i-ag7 with a bound hybrid insulin peptide
Structure deposition date
2021-12-13
Thiol separation (Å)
3
Half-sphere exposure sum ?
nan
Minimum pKa ?
9
% buried
22
Peptide A name
H-2 class II histocompatibility antigen, A-D alpha chain
Peptide B name
Insulin-1
Peptide A accession
P04228
Peptide B accession
P01325
Peptide A residue number
74
Peptide B residue number
107

Ligandability

Cysteine 74 of H-2 class II histocompatibility antigen, A-D alpha chain

Cysteine 107 of Insulin-1

Cysteine 74 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 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 alpha 1 chain between cysteines 132 and 188 (107 and 163 respectively in this structure).

Details

Redox score ?
79
PDB code
4ozg
Structure name
d2 protein complex
Structure deposition date
2014-02-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01909
Residue number A
132
Residue number B
188
Peptide name
HLA class II histocompatibility antigen, DQ alpha 1 chain

Ligandability

Cysteine 132 of HLA class II histocompatibility antigen, DQ alpha 1 chain

Cysteine 188 of HLA class II histocompatibility antigen, DQ alpha 1 chain

A redox-regulated disulphide may form within H-2 class II histocompatibility antigen, A-D alpha chain between cysteines 15 and 79.

Details

Redox score ?
nan
PDB code
1iao
Structure name
class ii mhc i-ad in complex with ovalbumin peptide 323-339
Structure deposition date
1998-03-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
88
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04228
Residue number A
15
Residue number B
79
Peptide name
H-2 class II histocompatibility antigen, A-D alpha chain

Ligandability

Cysteine 15 of H-2 class II histocompatibility antigen, A-D alpha chain

Cysteine 79 of H-2 class II histocompatibility antigen, A-D alpha chain

Cysteine 15 in protein A could not be asigned to a Uniprot residue.
Cysteine 79 in protein B could not be asigned to a Uniprot residue.
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