ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Protein polybromo-1

Intermolecular
Cysteine 450 and cysteine 450
Cysteine 736 and cysteine 736
Intramolecular
Cysteine 979 and cysteine 996
Cysteine 996 and cysteine 1059 L
Cysteine 979 and cysteine 1035
A redox-regulated disulphide may form between two units of Protein polybromo-1 at cysteines 450 and 450 (418 and 418 respectively in this structure).

Details

Redox score ?
79
PDB code
3k2j
Structure name
crystal structure of the 3rd bromodomain of human poly-bromodomain containing protein 1 (pb1)
Structure deposition date
2009-09-30
Thiol separation (Å)
2
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide A name
Protein polybromo-1
Peptide B name
Protein polybromo-1
Peptide A accession
Q86U86
Peptide B accession
Q86U86
Peptide A residue number
450
Peptide B residue number
450

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 between two units of Protein polybromo-1 at cysteines 736 and 736. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
5fh8
Structure name
crystal structure of the fifth bromodomain of human pb1 in complex with compound 28
Structure deposition date
2015-12-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
12
% buried
98
Peptide A name
Protein polybromo-1
Peptide B name
Protein polybromo-1
Peptide A accession
Q86U86
Peptide B accession
Q86U86
Peptide A residue number
736
Peptide B residue number
736

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 Protein polybromo-1 between cysteines 979 and 996. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
6oxb
Structure name
first bromo-adjacent homology (bah) domain of human polybromo-1 (pbrm1)
Structure deposition date
2019-05-13
Thiol separation (Å)
7
Half-sphere exposure sum ?
76
Minimum pKa ?
11
% buried
84
Peptide accession
Q86U86
Residue number A
979
Residue number B
996
Peptide name
Protein polybromo-1

Ligandability

Cysteine 979 of Protein polybromo-1

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 996 of Protein polybromo-1

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 Protein polybromo-1 between cysteines 996 and 1059. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
6oxb
Structure name
first bromo-adjacent homology (bah) domain of human polybromo-1 (pbrm1)
Structure deposition date
2019-05-13
Thiol separation (Å)
8
Half-sphere exposure sum ?
75
Minimum pKa ?
12
% buried
99
Peptide accession
Q86U86
Residue number A
996
Residue number B
1059
Peptide name
Protein polybromo-1

Ligandability

Cysteine 996 of Protein polybromo-1

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 1059 of Protein polybromo-1

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.

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 Protein polybromo-1 between cysteines 979 and 1035. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
26
PDB code
6oxb
Structure name
first bromo-adjacent homology (bah) domain of human polybromo-1 (pbrm1)
Structure deposition date
2019-05-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
78
Minimum pKa ?
13
% buried
96
Peptide accession
Q86U86
Residue number A
979
Residue number B
1035
Peptide name
Protein polybromo-1

Ligandability

Cysteine 979 of Protein polybromo-1

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 1035 of Protein polybromo-1

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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