ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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B-cell antigen receptor complex-associated protein beta chain

Intermolecular
Cysteine 113 of Yellow fluorescent protein and cysteine 135
Cysteine 119 of B-cell antigen receptor complex-associated protein alpha chain and cysteine 136
Cysteine 136 and cysteine 136
Intramolecular
Cysteine 43 and cysteine 135
Cysteine 43 and cysteine 126
Cysteine 65 and cysteine 122
Cysteine 43 and cysteine 65
Cysteine 43 and cysteine 120
Cysteine 122 and cysteine 136
Cysteine 65 and cysteine 136
A redox-regulated disulphide may form between cysteine 113 of Yellow fluorescent protein and cysteine 135 of B-cell antigen receptor complex-associated protein beta chain.

Details

Redox score ?
78
PDB code
8e4c
Structure name
igm bcr fab truncated form
Structure deposition date
2022-08-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide A name
Yellow fluorescent protein
Peptide B name
B-cell antigen receptor complex-associated protein beta chain
Peptide A accession
P21578
Peptide B accession
P15530
Peptide A residue number
113
Peptide B residue number
135

Ligandability

Cysteine 113 of Yellow fluorescent protein

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 135 of B-cell antigen receptor complex-associated protein beta 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 113 in protein A could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form between cysteine 119 of B-cell antigen receptor complex-associated protein alpha chain and cysteine 136 of B-cell antigen receptor complex-associated protein beta chain.

Details

Redox score ?
77
PDB code
7xt6
Structure name
structure of a membrane protein m3
Structure deposition date
2022-05-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide A name
B-cell antigen receptor complex-associated protein alpha chain
Peptide B name
B-cell antigen receptor complex-associated protein beta chain
Peptide A accession
P11912
Peptide B accession
P40259
Peptide A residue number
119
Peptide B residue number
136

Ligandability

Cysteine 119 of B-cell antigen receptor complex-associated protein alpha 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 136 of B-cell antigen receptor complex-associated protein beta 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 between two units of B-cell antigen receptor complex-associated protein beta chain at cysteines 136 and 136.

Details

Redox score ?
75
PDB code
3kg5
Structure name
crystal structure of human ig-beta homodimer
Structure deposition date
2009-10-28
Thiol separation (Å)
2
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide A name
B-cell antigen receptor complex-associated protein beta chain
Peptide B name
B-cell antigen receptor complex-associated protein beta chain
Peptide A accession
P40259
Peptide B accession
P40259
Peptide A residue number
136
Peptide B residue number
136

Ligandability

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 B-cell antigen receptor complex-associated protein beta chain between cysteines 43 and 135.

Details

Redox score ?
90
PDB code
3khq
Structure name
crystal structure of murine ig-beta (cd79b) in the monomeric form
Structure deposition date
2009-10-30
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15530
Residue number A
43
Residue number B
135
Peptide name
B-cell antigen receptor complex-associated protein beta chain

Ligandability

Cysteine 43 of B-cell antigen receptor complex-associated protein beta 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 135 of B-cell antigen receptor complex-associated protein beta 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 B-cell antigen receptor complex-associated protein beta chain between cysteines 43 and 126.

Details

Redox score ?
90
PDB code
3kg5
Structure name
crystal structure of human ig-beta homodimer
Structure deposition date
2009-10-28
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P40259
Residue number A
43
Residue number B
126
Peptide name
B-cell antigen receptor complex-associated protein beta chain

Ligandability

Cysteine 43 of B-cell antigen receptor complex-associated protein beta 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 126 of B-cell antigen receptor complex-associated protein beta 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 B-cell antigen receptor complex-associated protein beta chain between cysteines 65 and 122.

Details

Redox score ?
80
PDB code
3kg5
Structure name
crystal structure of human ig-beta homodimer
Structure deposition date
2009-10-28
Thiol separation (Å)
2
Half-sphere exposure sum ?
83
Minimum pKa ?
nan
% buried
nan
Peptide accession
P40259
Residue number A
65
Residue number B
122
Peptide name
B-cell antigen receptor complex-associated protein beta chain

Ligandability

Cysteine 65 of B-cell antigen receptor complex-associated protein beta 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 122 of B-cell antigen receptor complex-associated protein beta 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 B-cell antigen receptor complex-associated protein beta chain between cysteines 43 and 65. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
3khq
Structure name
crystal structure of murine ig-beta (cd79b) in the monomeric form
Structure deposition date
2009-10-30
Thiol separation (Å)
10
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15530
Residue number A
43
Residue number B
65
Peptide name
B-cell antigen receptor complex-associated protein beta chain

Ligandability

Cysteine 43 of B-cell antigen receptor complex-associated protein beta 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 65 of B-cell antigen receptor complex-associated protein beta 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 B-cell antigen receptor complex-associated protein beta chain between cysteines 43 and 120. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
3khq
Structure name
crystal structure of murine ig-beta (cd79b) in the monomeric form
Structure deposition date
2009-10-30
Thiol separation (Å)
10
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15530
Residue number A
43
Residue number B
120
Peptide name
B-cell antigen receptor complex-associated protein beta chain

Ligandability

Cysteine 43 of B-cell antigen receptor complex-associated protein beta 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 120 of B-cell antigen receptor complex-associated protein beta 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 B-cell antigen receptor complex-associated protein beta chain between cysteines 122 and 136. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
3kg5
Structure name
crystal structure of human ig-beta homodimer
Structure deposition date
2009-10-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
P40259
Residue number A
122
Residue number B
136
Peptide name
B-cell antigen receptor complex-associated protein beta chain

Ligandability

Cysteine 122 of B-cell antigen receptor complex-associated protein beta 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 136 of B-cell antigen receptor complex-associated protein beta 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 B-cell antigen receptor complex-associated protein beta chain between cysteines 65 and 136. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
3kg5
Structure name
crystal structure of human ig-beta homodimer
Structure deposition date
2009-10-28
Thiol separation (Å)
10
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
P40259
Residue number A
65
Residue number B
136
Peptide name
B-cell antigen receptor complex-associated protein beta chain

Ligandability

Cysteine 65 of B-cell antigen receptor complex-associated protein beta 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 136 of B-cell antigen receptor complex-associated protein beta 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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