ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Retinoblastoma-binding protein 5

Intramolecular
Cysteine 23 and cysteine 43
Cysteine 23 and cysteine 30
Cysteine 257 and cysteine 258
Cysteine 30 and cysteine 258
Cysteine 70 and cysteine 126
Cysteine 30 and cysteine 43
A redox-regulated disulphide may form within Retinoblastoma-binding protein 5 between cysteines 23 and 43.

Details

Redox score ?
68
PDB code
6km7
Structure name
the structural basis for the internal interaction in rbbp5
Structure deposition date
2019-07-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
88
Minimum pKa ?
8
% buried
100
Peptide accession
Q15291
Residue number A
23
Residue number B
43
Peptide name
Retinoblastoma-binding protein 5

Ligandability

Cysteine 23 of Retinoblastoma-binding protein 5

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 43 of Retinoblastoma-binding protein 5

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 Retinoblastoma-binding protein 5 between cysteines 23 and 30. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
6km7
Structure name
the structural basis for the internal interaction in rbbp5
Structure deposition date
2019-07-31
Thiol separation (Å)
9
Half-sphere exposure sum ?
90
Minimum pKa ?
8
% buried
100
Peptide accession
Q15291
Residue number A
23
Residue number B
30
Peptide name
Retinoblastoma-binding protein 5

Ligandability

Cysteine 23 of Retinoblastoma-binding protein 5

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 30 of Retinoblastoma-binding protein 5

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 Retinoblastoma-binding protein 5 between cysteines 257 and 258. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
5ov3
Structure name
structure of the rbbp5 beta-propeller domain
Structure deposition date
2017-08-27
Thiol separation (Å)
7
Half-sphere exposure sum ?
90
Minimum pKa ?
11
% buried
100
Peptide accession
Q8BX09
Residue number A
257
Residue number B
258
Peptide name
Retinoblastoma-binding protein 5

Ligandability

Cysteine 257 of Retinoblastoma-binding protein 5

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 258 of Retinoblastoma-binding protein 5

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 Retinoblastoma-binding protein 5 between cysteines 30 and 258. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
6km7
Structure name
the structural basis for the internal interaction in rbbp5
Structure deposition date
2019-07-31
Thiol separation (Å)
8
Half-sphere exposure sum ?
90
Minimum pKa ?
12
% buried
100
Peptide accession
Q15291
Residue number A
30
Residue number B
258
Peptide name
Retinoblastoma-binding protein 5

Ligandability

Cysteine 30 of Retinoblastoma-binding protein 5

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 258 of Retinoblastoma-binding protein 5

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 Retinoblastoma-binding protein 5 between cysteines 70 and 126. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
26
PDB code
6pwv
Structure name
cryo-em structure of mll1 core complex bound to the nucleosome
Structure deposition date
2019-07-23
Thiol separation (Å)
10
Half-sphere exposure sum ?
84
Minimum pKa ?
10
% buried
82
Peptide accession
Q15291
Residue number A
70
Residue number B
126
Peptide name
Retinoblastoma-binding protein 5

Ligandability

Cysteine 70 of Retinoblastoma-binding protein 5

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 Retinoblastoma-binding protein 5

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 Retinoblastoma-binding protein 5 between cysteines 30 and 43. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
24
PDB code
6km7
Structure name
the structural basis for the internal interaction in rbbp5
Structure deposition date
2019-07-31
Thiol separation (Å)
10
Half-sphere exposure sum ?
91
Minimum pKa ?
14
% buried
100
Peptide accession
Q15291
Residue number A
30
Residue number B
43
Peptide name
Retinoblastoma-binding protein 5

Ligandability

Cysteine 30 of Retinoblastoma-binding protein 5

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 43 of Retinoblastoma-binding protein 5

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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