ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Breast cancer type 1 susceptibility protein

Intramolecular
Cysteine 24 and cysteine 27
Cysteine 24 and cysteine 44 L
Cysteine 61 and cysteine 64 L
Cysteine 39 and cysteine 64 L
Cysteine 24 and cysteine 47
Cysteine 39 and cysteine 61 L
Cysteine 44 and cysteine 47 L
Cysteine 27 and cysteine 47
Cysteine 27 and cysteine 44 L
Cysteine 1767 and cysteine 1828
More...
Cysteine 1767 and cysteine 1768
Cysteine 1713 and cysteine 1714
Cysteine 1787 and cysteine 1847
A redox-regulated disulphide may form within Breast cancer type 1 susceptibility protein between cysteines 24 and 27.

Details

Redox score ?
89
PDB code
1jm7
Structure name
solution structure of the brca1/bard1 ring-domain heterodimer
Structure deposition date
2001-07-17
Thiol separation (Å)
3
Half-sphere exposure sum ?
47
Minimum pKa ?
6
% buried
16
Peptide accession
P38398
Residue number A
24
Residue number B
27
Peptide name
Breast cancer type 1 susceptibility protein

Ligandability

Cysteine 24 of Breast cancer type 1 susceptibility 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 27 of Breast cancer type 1 susceptibility 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.

A redox-regulated disulphide may form within Breast cancer type 1 susceptibility protein between cysteines 24 and 44.

Details

Redox score ?
84
PDB code
1jm7
Structure name
solution structure of the brca1/bard1 ring-domain heterodimer
Structure deposition date
2001-07-17
Thiol separation (Å)
3
Half-sphere exposure sum ?
63
Minimum pKa ?
6
% buried
32
Peptide accession
P38398
Residue number A
24
Residue number B
44
Peptide name
Breast cancer type 1 susceptibility protein

Ligandability

Cysteine 24 of Breast cancer type 1 susceptibility 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 44 of Breast cancer type 1 susceptibility 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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Breast cancer type 1 susceptibility protein between cysteines 61 and 64.

Details

Redox score ?
84
PDB code
1jm7
Structure name
solution structure of the brca1/bard1 ring-domain heterodimer
Structure deposition date
2001-07-17
Thiol separation (Å)
3
Half-sphere exposure sum ?
42
Minimum pKa ?
8
% buried
15
Peptide accession
P38398
Residue number A
61
Residue number B
64
Peptide name
Breast cancer type 1 susceptibility protein

Ligandability

Cysteine 61 of Breast cancer type 1 susceptibility 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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 64 of Breast cancer type 1 susceptibility 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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Breast cancer type 1 susceptibility protein between cysteines 39 and 64.

Details

Redox score ?
82
PDB code
1jm7
Structure name
solution structure of the brca1/bard1 ring-domain heterodimer
Structure deposition date
2001-07-17
Thiol separation (Å)
3
Half-sphere exposure sum ?
44
Minimum pKa ?
8
% buried
10
Peptide accession
P38398
Residue number A
39
Residue number B
64
Peptide name
Breast cancer type 1 susceptibility protein

Ligandability

Cysteine 39 of Breast cancer type 1 susceptibility 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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 64 of Breast cancer type 1 susceptibility 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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Breast cancer type 1 susceptibility protein between cysteines 24 and 47.

Details

Redox score ?
80
PDB code
1jm7
Structure name
solution structure of the brca1/bard1 ring-domain heterodimer
Structure deposition date
2001-07-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
6
% buried
32
Peptide accession
P38398
Residue number A
24
Residue number B
47
Peptide name
Breast cancer type 1 susceptibility protein

Ligandability

Cysteine 24 of Breast cancer type 1 susceptibility 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 47 of Breast cancer type 1 susceptibility 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.

A redox-regulated disulphide may form within Breast cancer type 1 susceptibility protein between cysteines 39 and 61.

Details

Redox score ?
76
PDB code
1jm7
Structure name
solution structure of the brca1/bard1 ring-domain heterodimer
Structure deposition date
2001-07-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
9
% buried
26
Peptide accession
P38398
Residue number A
39
Residue number B
61
Peptide name
Breast cancer type 1 susceptibility protein

Ligandability

Cysteine 39 of Breast cancer type 1 susceptibility 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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 61 of Breast cancer type 1 susceptibility 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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Breast cancer type 1 susceptibility protein between cysteines 44 and 47.

Details

Redox score ?
74
PDB code
1jm7
Structure name
solution structure of the brca1/bard1 ring-domain heterodimer
Structure deposition date
2001-07-17
Thiol separation (Å)
3
Half-sphere exposure sum ?
67
Minimum pKa ?
9
% buried
35
Peptide accession
P38398
Residue number A
44
Residue number B
47
Peptide name
Breast cancer type 1 susceptibility protein

Ligandability

Cysteine 44 of Breast cancer type 1 susceptibility 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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 47 of Breast cancer type 1 susceptibility 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.

A redox-regulated disulphide may form within Breast cancer type 1 susceptibility protein between cysteines 27 and 47.

Details

Redox score ?
73
PDB code
1jm7
Structure name
solution structure of the brca1/bard1 ring-domain heterodimer
Structure deposition date
2001-07-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
9
% buried
20
Peptide accession
P38398
Residue number A
27
Residue number B
47
Peptide name
Breast cancer type 1 susceptibility protein

Ligandability

Cysteine 27 of Breast cancer type 1 susceptibility 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 47 of Breast cancer type 1 susceptibility 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.

A redox-regulated disulphide may form within Breast cancer type 1 susceptibility protein between cysteines 27 and 44.

Details

Redox score ?
68
PDB code
1jm7
Structure name
solution structure of the brca1/bard1 ring-domain heterodimer
Structure deposition date
2001-07-17
Thiol separation (Å)
5
Half-sphere exposure sum ?
52
Minimum pKa ?
10
% buried
20
Peptide accession
P38398
Residue number A
27
Residue number B
44
Peptide name
Breast cancer type 1 susceptibility protein

Ligandability

Cysteine 27 of Breast cancer type 1 susceptibility 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 44 of Breast cancer type 1 susceptibility 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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Breast cancer type 1 susceptibility protein between cysteines 1767 and 1828. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
4igk
Structure name
structure of human brca1 brct in complex with atrip peptide
Structure deposition date
2012-12-17
Thiol separation (Å)
8
Half-sphere exposure sum ?
62
Minimum pKa ?
9
% buried
36
Peptide accession
P38398
Residue number A
1767
Residue number B
1828
Peptide name
Breast cancer type 1 susceptibility protein

Ligandability

Cysteine 1767 of Breast cancer type 1 susceptibility 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 1828 of Breast cancer type 1 susceptibility 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.

A redox-regulated disulphide may form within Breast cancer type 1 susceptibility protein between cysteines 1767 and 1768. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
3coj
Structure name
crystal structure of the brct domains of human brca1 in complex with a phosphorylated peptide from human acetyl-coa carboxylase 1
Structure deposition date
2008-03-28
Thiol separation (Å)
7
Half-sphere exposure sum ?
79
Minimum pKa ?
11
% buried
74
Peptide accession
P38398
Residue number A
1767
Residue number B
1768
Peptide name
Breast cancer type 1 susceptibility protein

Ligandability

Cysteine 1767 of Breast cancer type 1 susceptibility 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 1768 of Breast cancer type 1 susceptibility 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.

A redox-regulated disulphide may form within Breast cancer type 1 susceptibility protein homolog between cysteines 1713 and 1714. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
1l0b
Structure name
crystal structure of rat brca1 tandem-brct region
Structure deposition date
2002-02-08
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
10
% buried
32
Peptide accession
O54952
Residue number A
1713
Residue number B
1714
Peptide name
Breast cancer type 1 susceptibility protein homolog

Ligandability

Cysteine 1713 of Breast cancer type 1 susceptibility protein homolog

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 1714 of Breast cancer type 1 susceptibility protein homolog

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 Breast cancer type 1 susceptibility protein between cysteines 1787 and 1847. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
1t2v
Structure name
structural basis of phospho-peptide recognition by the brct domain of brca1, structure with phosphopeptide
Structure deposition date
2004-04-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
11
% buried
64
Peptide accession
P38398
Residue number A
1787
Residue number B
1847
Peptide name
Breast cancer type 1 susceptibility protein

Ligandability

Cysteine 1787 of Breast cancer type 1 susceptibility 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 1847 of Breast cancer type 1 susceptibility 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.

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