ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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E3 ubiquitin-protein ligase UHRF2

Intermolecular
Cysteine 704 and cysteine 704
Intramolecular
Cysteine 362 and cysteine 392
Cysteine 389 and cysteine 392
Cysteine 331 and cysteine 334
Cysteine 334 and cysteine 342
Cysteine 331 and cysteine 342
Cysteine 365 and cysteine 392
Cysteine 362 and cysteine 389
Cysteine 334 and cysteine 345 L
Cysteine 362 and cysteine 365
More...
Cysteine 342 and cysteine 345 L
Cysteine 365 and cysteine 389
Cysteine 331 and cysteine 345 L
Cysteine 347 and cysteine 350
Cysteine 347 and cysteine 373
Cysteine 350 and cysteine 373
A redox-regulated disulphide may form between two units of E3 ubiquitin-protein ligase UHRF2 at cysteines 704 and 704.

Details

Redox score ?
71
PDB code
1z6u
Structure name
np95-like ring finger protein isoform b [homo sapiens]
Structure deposition date
2005-03-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
7
% buried
72
Peptide A name
E3 ubiquitin-protein ligase UHRF2
Peptide B name
E3 ubiquitin-protein ligase UHRF2
Peptide A accession
Q96PU4
Peptide B accession
Q96PU4
Peptide A residue number
704
Peptide B residue number
704

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 E3 ubiquitin-protein ligase UHRF2 between cysteines 362 and 392 (44 and 74 respectively in this structure).

Details

Redox score ?
90
PDB code
2e6s
Structure name
solution structure of the phd domain in ring finger protein 107
Structure deposition date
2006-12-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
38
Minimum pKa ?
5
% buried
0
Peptide accession
Q96PU4
Residue number A
362
Residue number B
392
Peptide name
E3 ubiquitin-protein ligase UHRF2

Ligandability

Cysteine 362 of E3 ubiquitin-protein ligase UHRF2

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 392 of E3 ubiquitin-protein ligase UHRF2

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 E3 ubiquitin-protein ligase UHRF2 between cysteines 389 and 392 (71 and 74 respectively in this structure).

Details

Redox score ?
84
PDB code
2e6s
Structure name
solution structure of the phd domain in ring finger protein 107
Structure deposition date
2006-12-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
8
% buried
4
Peptide accession
Q96PU4
Residue number A
389
Residue number B
392
Peptide name
E3 ubiquitin-protein ligase UHRF2

Ligandability

Cysteine 389 of E3 ubiquitin-protein ligase UHRF2

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 392 of E3 ubiquitin-protein ligase UHRF2

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 E3 ubiquitin-protein ligase UHRF2 between cysteines 331 and 334.

Details

Redox score ?
81
PDB code
4tvr
Structure name
tandem tudor and phd domains of uhrf2
Structure deposition date
2014-06-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96PU4
Residue number A
331
Residue number B
334
Peptide name
E3 ubiquitin-protein ligase UHRF2

Ligandability

Cysteine 331 of E3 ubiquitin-protein ligase UHRF2

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 334 of E3 ubiquitin-protein ligase UHRF2

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 E3 ubiquitin-protein ligase UHRF2 between cysteines 334 and 342.

Details

Redox score ?
79
PDB code
4tvr
Structure name
tandem tudor and phd domains of uhrf2
Structure deposition date
2014-06-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
43
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96PU4
Residue number A
334
Residue number B
342
Peptide name
E3 ubiquitin-protein ligase UHRF2

Ligandability

Cysteine 334 of E3 ubiquitin-protein ligase UHRF2

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 342 of E3 ubiquitin-protein ligase UHRF2

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 E3 ubiquitin-protein ligase UHRF2 between cysteines 331 and 342.

Details

Redox score ?
79
PDB code
4tvr
Structure name
tandem tudor and phd domains of uhrf2
Structure deposition date
2014-06-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96PU4
Residue number A
331
Residue number B
342
Peptide name
E3 ubiquitin-protein ligase UHRF2

Ligandability

Cysteine 331 of E3 ubiquitin-protein ligase UHRF2

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 342 of E3 ubiquitin-protein ligase UHRF2

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 E3 ubiquitin-protein ligase UHRF2 between cysteines 365 and 392 (47 and 74 respectively in this structure).

Details

Redox score ?
78
PDB code
2e6s
Structure name
solution structure of the phd domain in ring finger protein 107
Structure deposition date
2006-12-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
33
Minimum pKa ?
10
% buried
0
Peptide accession
Q96PU4
Residue number A
365
Residue number B
392
Peptide name
E3 ubiquitin-protein ligase UHRF2

Ligandability

Cysteine 365 of E3 ubiquitin-protein ligase UHRF2

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 392 of E3 ubiquitin-protein ligase UHRF2

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 E3 ubiquitin-protein ligase UHRF2 between cysteines 362 and 389.

Details

Redox score ?
78
PDB code
4tvr
Structure name
tandem tudor and phd domains of uhrf2
Structure deposition date
2014-06-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
45
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96PU4
Residue number A
362
Residue number B
389
Peptide name
E3 ubiquitin-protein ligase UHRF2

Ligandability

Cysteine 362 of E3 ubiquitin-protein ligase UHRF2

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 389 of E3 ubiquitin-protein ligase UHRF2

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 E3 ubiquitin-protein ligase UHRF2 between cysteines 334 and 345.

Details

Redox score ?
77
PDB code
4tvr
Structure name
tandem tudor and phd domains of uhrf2
Structure deposition date
2014-06-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96PU4
Residue number A
334
Residue number B
345
Peptide name
E3 ubiquitin-protein ligase UHRF2

Ligandability

Cysteine 334 of E3 ubiquitin-protein ligase UHRF2

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 345 of E3 ubiquitin-protein ligase UHRF2

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase UHRF2 between cysteines 362 and 365.

Details

Redox score ?
77
PDB code
4tvr
Structure name
tandem tudor and phd domains of uhrf2
Structure deposition date
2014-06-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
36
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96PU4
Residue number A
362
Residue number B
365
Peptide name
E3 ubiquitin-protein ligase UHRF2

Ligandability

Cysteine 362 of E3 ubiquitin-protein ligase UHRF2

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 365 of E3 ubiquitin-protein ligase UHRF2

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 E3 ubiquitin-protein ligase UHRF2 between cysteines 342 and 345.

Details

Redox score ?
76
PDB code
4tvr
Structure name
tandem tudor and phd domains of uhrf2
Structure deposition date
2014-06-27
Thiol separation (Å)
3
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96PU4
Residue number A
342
Residue number B
345
Peptide name
E3 ubiquitin-protein ligase UHRF2

Ligandability

Cysteine 342 of E3 ubiquitin-protein ligase UHRF2

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 345 of E3 ubiquitin-protein ligase UHRF2

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase UHRF2 between cysteines 365 and 389.

Details

Redox score ?
75
PDB code
4tvr
Structure name
tandem tudor and phd domains of uhrf2
Structure deposition date
2014-06-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
39
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96PU4
Residue number A
365
Residue number B
389
Peptide name
E3 ubiquitin-protein ligase UHRF2

Ligandability

Cysteine 365 of E3 ubiquitin-protein ligase UHRF2

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 389 of E3 ubiquitin-protein ligase UHRF2

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 E3 ubiquitin-protein ligase UHRF2 between cysteines 331 and 345.

Details

Redox score ?
75
PDB code
4tvr
Structure name
tandem tudor and phd domains of uhrf2
Structure deposition date
2014-06-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96PU4
Residue number A
331
Residue number B
345
Peptide name
E3 ubiquitin-protein ligase UHRF2

Ligandability

Cysteine 331 of E3 ubiquitin-protein ligase UHRF2

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 345 of E3 ubiquitin-protein ligase UHRF2

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase UHRF2 between cysteines 347 and 350.

Details

Redox score ?
75
PDB code
4tvr
Structure name
tandem tudor and phd domains of uhrf2
Structure deposition date
2014-06-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96PU4
Residue number A
347
Residue number B
350
Peptide name
E3 ubiquitin-protein ligase UHRF2

Ligandability

Cysteine 347 of E3 ubiquitin-protein ligase UHRF2

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 350 of E3 ubiquitin-protein ligase UHRF2

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 E3 ubiquitin-protein ligase UHRF2 between cysteines 347 and 373.

Details

Redox score ?
74
PDB code
4tvr
Structure name
tandem tudor and phd domains of uhrf2
Structure deposition date
2014-06-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96PU4
Residue number A
347
Residue number B
373
Peptide name
E3 ubiquitin-protein ligase UHRF2

Ligandability

Cysteine 347 of E3 ubiquitin-protein ligase UHRF2

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 373 of E3 ubiquitin-protein ligase UHRF2

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 E3 ubiquitin-protein ligase UHRF2 between cysteines 350 and 373.

Details

Redox score ?
71
PDB code
4tvr
Structure name
tandem tudor and phd domains of uhrf2
Structure deposition date
2014-06-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
43
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96PU4
Residue number A
350
Residue number B
373
Peptide name
E3 ubiquitin-protein ligase UHRF2

Ligandability

Cysteine 350 of E3 ubiquitin-protein ligase UHRF2

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 373 of E3 ubiquitin-protein ligase UHRF2

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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