ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Apoptosis-resistant E3 ubiquitin protein ligase 1

Intramolecular
Cysteine 515 and cysteine 562
Cysteine 611 and cysteine 790
Cysteine 515 and cysteine 705
Cysteine 562 and cysteine 705
A redox-regulated disulphide may form within Apoptosis-resistant E3 ubiquitin protein ligase 1 between cysteines 515 and 562.

Details

Redox score ?
66
PDB code
6jx5
Structure name
hect domain of arel1
Structure deposition date
2019-04-22
Thiol separation (Å)
5
Half-sphere exposure sum ?
76
Minimum pKa ?
8
% buried
100
Peptide accession
O15033
Residue number A
515
Residue number B
562
Peptide name
Apoptosis-resistant E3 ubiquitin protein ligase 1

Ligandability

Cysteine 515 of Apoptosis-resistant E3 ubiquitin protein ligase 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 562 of Apoptosis-resistant E3 ubiquitin protein ligase 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 Apoptosis-resistant E3 ubiquitin protein ligase 1 between cysteines 611 and 790. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
6loh
Structure name
crystal structure of the catalytic domain of human ubiquitin ligase arel1
Structure deposition date
2020-01-05
Thiol separation (Å)
6
Half-sphere exposure sum ?
62
Minimum pKa ?
11
% buried
67
Peptide accession
O15033
Residue number A
611
Residue number B
790
Peptide name
Apoptosis-resistant E3 ubiquitin protein ligase 1

Ligandability

Cysteine 611 of Apoptosis-resistant E3 ubiquitin protein ligase 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 790 of Apoptosis-resistant E3 ubiquitin protein ligase 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 Apoptosis-resistant E3 ubiquitin protein ligase 1 between cysteines 515 and 705. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
6loh
Structure name
crystal structure of the catalytic domain of human ubiquitin ligase arel1
Structure deposition date
2020-01-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
70
Minimum pKa ?
8
% buried
98
Peptide accession
O15033
Residue number A
515
Residue number B
705
Peptide name
Apoptosis-resistant E3 ubiquitin protein ligase 1

Ligandability

Cysteine 515 of Apoptosis-resistant E3 ubiquitin protein ligase 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 705 of Apoptosis-resistant E3 ubiquitin protein ligase 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 Apoptosis-resistant E3 ubiquitin protein ligase 1 between cysteines 562 and 705. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
29
PDB code
6loh
Structure name
crystal structure of the catalytic domain of human ubiquitin ligase arel1
Structure deposition date
2020-01-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
14
% buried
100
Peptide accession
O15033
Residue number A
562
Residue number B
705
Peptide name
Apoptosis-resistant E3 ubiquitin protein ligase 1

Ligandability

Cysteine 562 of Apoptosis-resistant E3 ubiquitin protein ligase 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 705 of Apoptosis-resistant E3 ubiquitin protein ligase 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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