ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Tonsoku-like protein

Intramolecular
Cysteine 561 and cysteine 596
Cysteine 570 and cysteine 608
Cysteine 537 and cysteine 570
A redox-regulated disulphide may form within Tonsoku-like protein between cysteines 561 and 596.

Details

Redox score ?
68
PDB code
5ja4
Structure name
crystal structure of human tonsl and mcm2 hbds binding to a histone h3-h4 tetramer
Structure deposition date
2016-04-11
Thiol separation (Å)
5
Half-sphere exposure sum ?
53
Minimum pKa ?
10
% buried
37
Peptide accession
Q96HA7
Residue number A
561
Residue number B
596
Peptide name
Tonsoku-like protein

Ligandability

Cysteine 561 of Tonsoku-like 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 596 of Tonsoku-like 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 Tonsoku-like protein between cysteines 570 and 608. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
5ja4
Structure name
crystal structure of human tonsl and mcm2 hbds binding to a histone h3-h4 tetramer
Structure deposition date
2016-04-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
83
Minimum pKa ?
12
% buried
85
Peptide accession
Q96HA7
Residue number A
570
Residue number B
608
Peptide name
Tonsoku-like protein

Ligandability

Cysteine 570 of Tonsoku-like 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 608 of Tonsoku-like 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 Tonsoku-like protein between cysteines 537 and 570. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
PDB code
5ja4
Structure name
crystal structure of human tonsl and mcm2 hbds binding to a histone h3-h4 tetramer
Structure deposition date
2016-04-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
87
Minimum pKa ?
13
% buried
100
Peptide accession
Q96HA7
Residue number A
537
Residue number B
570
Peptide name
Tonsoku-like protein

Ligandability

Cysteine 537 of Tonsoku-like 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 570 of Tonsoku-like 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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