ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Breakpoint cluster region protein

Intramolecular
Cysteine 608 and cysteine 609
Cysteine 753 and cysteine 886
Cysteine 737 and cysteine 753
A redox-regulated disulphide may form within Breakpoint cluster region protein between cysteines 608 and 609. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
5n7e
Structure name
crystal structure of the dbl-homology domain of bcr-abl in complex with monobody mb(bcr-dh_4)
Structure deposition date
2017-02-20
Thiol separation (Å)
7
Half-sphere exposure sum ?
51
Minimum pKa ?
10
% buried
26
Peptide accession
P11274
Residue number A
608
Residue number B
609
Peptide name
Breakpoint cluster region protein

Ligandability

Cysteine 608 of Breakpoint cluster region 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 609 of Breakpoint cluster region 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 Breakpoint cluster region protein between cysteines 753 and 886. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
5oc7
Structure name
crystal structure of the pleckstrin-homology domain of bcr-abl in complex with monobody mb(bcr-ph_4)
Structure deposition date
2017-06-29
Thiol separation (Å)
10
Half-sphere exposure sum ?
nan
Minimum pKa ?
9
% buried
35
Peptide accession
P11274
Residue number A
753
Residue number B
886
Peptide name
Breakpoint cluster region protein

Ligandability

Cysteine 753 of Breakpoint cluster region 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 886 of Breakpoint cluster region 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 Breakpoint cluster region protein between cysteines 737 and 753. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
5oc7
Structure name
crystal structure of the pleckstrin-homology domain of bcr-abl in complex with monobody mb(bcr-ph_4)
Structure deposition date
2017-06-29
Thiol separation (Å)
9
Half-sphere exposure sum ?
65
Minimum pKa ?
11
% buried
68
Peptide accession
P11274
Residue number A
737
Residue number B
753
Peptide name
Breakpoint cluster region protein

Ligandability

Cysteine 737 of Breakpoint cluster region 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 753 of Breakpoint cluster region 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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