ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Probable E3 ubiquitin-protein ligase DTX2

Intramolecular
Cysteine 445 and cysteine 472
Cysteine 466 and cysteine 469
Cysteine 412 and cysteine 415
Cysteine 445 and cysteine 469
Cysteine 412 and cysteine 453
Cysteine 415 and cysteine 453
Cysteine 412 and cysteine 469
A redox-regulated disulphide may form within Probable E3 ubiquitin-protein ligase DTX2 between cysteines 445 and 472 (47 and 74 respectively in this structure).

Details

Redox score ?
81
PDB code
6ir0
Structure name
zinc finger domain of the human dtx protein
Structure deposition date
2018-11-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
35
Minimum pKa ?
7
% buried
4
Peptide accession
Q86UW9
Residue number A
445
Residue number B
472
Peptide name
Probable E3 ubiquitin-protein ligase DTX2

Ligandability

Cysteine 445 of Probable E3 ubiquitin-protein ligase DTX2

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 472 of Probable E3 ubiquitin-protein ligase DTX2

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 Probable E3 ubiquitin-protein ligase DTX2 between cysteines 466 and 469 (85 and 88 respectively in this structure).

Details

Redox score ?
81
PDB code
1v87
Structure name
solution structure of the ring-h2 finger domain of mouse deltex protein 2
Structure deposition date
2003-12-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
6
% buried
21
Peptide accession
Q8R3P2
Residue number A
466
Residue number B
469
Peptide name
Probable E3 ubiquitin-protein ligase DTX2

Ligandability

Cysteine 466 of Probable E3 ubiquitin-protein ligase DTX2

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 469 of Probable E3 ubiquitin-protein ligase DTX2

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 Probable E3 ubiquitin-protein ligase DTX2 between cysteines 412 and 415 (14 and 17 respectively in this structure).

Details

Redox score ?
79
PDB code
6ir0
Structure name
zinc finger domain of the human dtx protein
Structure deposition date
2018-11-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
8
% buried
30
Peptide accession
Q86UW9
Residue number A
412
Residue number B
415
Peptide name
Probable E3 ubiquitin-protein ligase DTX2

Ligandability

Cysteine 412 of Probable E3 ubiquitin-protein ligase DTX2

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 415 of Probable E3 ubiquitin-protein ligase DTX2

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 Probable E3 ubiquitin-protein ligase DTX2 between cysteines 445 and 469 (47 and 71 respectively in this structure).

Details

Redox score ?
79
PDB code
6ir0
Structure name
zinc finger domain of the human dtx protein
Structure deposition date
2018-11-09
Thiol separation (Å)
3
Half-sphere exposure sum ?
55
Minimum pKa ?
8
% buried
17
Peptide accession
Q86UW9
Residue number A
445
Residue number B
469
Peptide name
Probable E3 ubiquitin-protein ligase DTX2

Ligandability

Cysteine 445 of Probable E3 ubiquitin-protein ligase DTX2

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 469 of Probable E3 ubiquitin-protein ligase DTX2

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 Probable E3 ubiquitin-protein ligase DTX2 between cysteines 412 and 453 (14 and 55 respectively in this structure).

Details

Redox score ?
74
PDB code
6ir0
Structure name
zinc finger domain of the human dtx protein
Structure deposition date
2018-11-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
78
Minimum pKa ?
8
% buried
42
Peptide accession
Q86UW9
Residue number A
412
Residue number B
453
Peptide name
Probable E3 ubiquitin-protein ligase DTX2

Ligandability

Cysteine 412 of Probable E3 ubiquitin-protein ligase DTX2

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 453 of Probable E3 ubiquitin-protein ligase DTX2

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 Probable E3 ubiquitin-protein ligase DTX2 between cysteines 415 and 453 (17 and 55 respectively in this structure).

Details

Redox score ?
72
PDB code
6ir0
Structure name
zinc finger domain of the human dtx protein
Structure deposition date
2018-11-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
8
% buried
28
Peptide accession
Q86UW9
Residue number A
415
Residue number B
453
Peptide name
Probable E3 ubiquitin-protein ligase DTX2

Ligandability

Cysteine 415 of Probable E3 ubiquitin-protein ligase DTX2

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 453 of Probable E3 ubiquitin-protein ligase DTX2

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 Probable E3 ubiquitin-protein ligase DTX2 between cysteines 412 and 469 (14 and 71 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
6ir0
Structure name
zinc finger domain of the human dtx protein
Structure deposition date
2018-11-09
Thiol separation (Å)
10
Half-sphere exposure sum ?
72
Minimum pKa ?
8
% buried
35
Peptide accession
Q86UW9
Residue number A
412
Residue number B
469
Peptide name
Probable E3 ubiquitin-protein ligase DTX2

Ligandability

Cysteine 412 of Probable E3 ubiquitin-protein ligase DTX2

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 469 of Probable E3 ubiquitin-protein ligase DTX2

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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