ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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E3 ubiquitin-protein ligase UHRF1

Intermolecular
Cysteine 321 and cysteine 321
Cysteine 344 and cysteine 344
Intramolecular
Cysteine 333 and cysteine 336
Cysteine 724 and cysteine 727
Cysteine 302 and cysteine 313
Cysteine 724 and cysteine 726
Cysteine 724 and cysteine 747
Cysteine 724 and cysteine 744
Cysteine 333 and cysteine 363
Cysteine 302 and cysteine 305
More...
Cysteine 313 and cysteine 316
Cysteine 739 and cysteine 759
Cysteine 305 and cysteine 316
Cysteine 305 and cysteine 313
Cysteine 318 and cysteine 321
Cysteine 333 and cysteine 360
Cysteine 759 and cysteine 762
Cysteine 739 and cysteine 762
Cysteine 336 and cysteine 363
Cysteine 302 and cysteine 316
Cysteine 318 and cysteine 344
Cysteine 360 and cysteine 363
Cysteine 727 and cysteine 747
Cysteine 336 and cysteine 360
Cysteine 727 and cysteine 744
Cysteine 321 and cysteine 344
Cysteine 744 and cysteine 747
Cysteine 726 and cysteine 747
Cysteine 726 and cysteine 727
Cysteine 240 and cysteine 266
Cysteine 726 and cysteine 759
Cysteine 724 and cysteine 759
Cysteine 318 and cysteine 360
Cysteine 726 and cysteine 744
Cysteine 313 and cysteine 321
Cysteine 313 and cysteine 318
A redox-regulated disulphide may form between two units of E3 ubiquitin-protein ligase UHRF1 at cysteines 321 and 321. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
3zvy
Structure name
phd finger of human uhrf1 in complex with unmodified histone h3 n- terminal tail
Structure deposition date
2011-07-28
Thiol separation (Å)
7
Half-sphere exposure sum ?
65
Minimum pKa ?
8
% buried
82
Peptide A name
E3 ubiquitin-protein ligase UHRF1
Peptide B name
E3 ubiquitin-protein ligase UHRF1
Peptide A accession
Q96T88
Peptide B accession
Q96T88
Peptide A residue number
321
Peptide B residue number
321

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 between two units of E3 ubiquitin-protein ligase UHRF1 at cysteines 344 and 344. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
21
PDB code
3zvy
Structure name
phd finger of human uhrf1 in complex with unmodified histone h3 n- terminal tail
Structure deposition date
2011-07-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
66
Minimum pKa ?
19
% buried
82
Peptide A name
E3 ubiquitin-protein ligase UHRF1
Peptide B name
E3 ubiquitin-protein ligase UHRF1
Peptide A accession
Q96T88
Peptide B accession
Q96T88
Peptide A residue number
344
Peptide B residue number
344

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 UHRF1 between cysteines 333 and 336.

Details

Redox score ?
93
PDB code
3ask
Structure name
structure of uhrf1 in complex with histone tail
Structure deposition date
2010-12-16
Thiol separation (Å)
3
Half-sphere exposure sum ?
46
Minimum pKa ?
4
% buried
0
Peptide accession
Q96T88
Residue number A
333
Residue number B
336
Peptide name
E3 ubiquitin-protein ligase UHRF1

Ligandability

Cysteine 333 of E3 ubiquitin-protein ligase UHRF1

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 336 of E3 ubiquitin-protein ligase UHRF1

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 UHRF1 between cysteines 724 and 727.

Details

Redox score ?
91
PDB code
3fl2
Structure name
crystal structure of the ring domain of the e3 ubiquitin-protein ligase uhrf1
Structure deposition date
2008-12-18
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
3
% buried
36
Peptide accession
Q96T88
Residue number A
724
Residue number B
727
Peptide name
E3 ubiquitin-protein ligase UHRF1

Ligandability

Cysteine 724 of E3 ubiquitin-protein ligase UHRF1

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 727 of E3 ubiquitin-protein ligase UHRF1

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 UHRF1 between cysteines 302 and 313.

Details

Redox score ?
88
PDB code
3ask
Structure name
structure of uhrf1 in complex with histone tail
Structure deposition date
2010-12-16
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
6
% buried
4
Peptide accession
Q96T88
Residue number A
302
Residue number B
313
Peptide name
E3 ubiquitin-protein ligase UHRF1

Ligandability

Cysteine 302 of E3 ubiquitin-protein ligase UHRF1

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 313 of E3 ubiquitin-protein ligase UHRF1

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 UHRF1 between cysteines 724 and 726.

Details

Redox score ?
88
PDB code
3fl2
Structure name
crystal structure of the ring domain of the e3 ubiquitin-protein ligase uhrf1
Structure deposition date
2008-12-18
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
3
% buried
42
Peptide accession
Q96T88
Residue number A
724
Residue number B
726
Peptide name
E3 ubiquitin-protein ligase UHRF1

Ligandability

Cysteine 724 of E3 ubiquitin-protein ligase UHRF1

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 726 of E3 ubiquitin-protein ligase UHRF1

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 UHRF1 between cysteines 724 and 747.

Details

Redox score ?
88
PDB code
3fl2
Structure name
crystal structure of the ring domain of the e3 ubiquitin-protein ligase uhrf1
Structure deposition date
2008-12-18
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
3
% buried
40
Peptide accession
Q96T88
Residue number A
724
Residue number B
747
Peptide name
E3 ubiquitin-protein ligase UHRF1

Ligandability

Cysteine 724 of E3 ubiquitin-protein ligase UHRF1

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 747 of E3 ubiquitin-protein ligase UHRF1

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 UHRF1 between cysteines 724 and 744.

Details

Redox score ?
88
PDB code
3fl2
Structure name
crystal structure of the ring domain of the e3 ubiquitin-protein ligase uhrf1
Structure deposition date
2008-12-18
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
3
% buried
52
Peptide accession
Q96T88
Residue number A
724
Residue number B
744
Peptide name
E3 ubiquitin-protein ligase UHRF1

Ligandability

Cysteine 724 of E3 ubiquitin-protein ligase UHRF1

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 744 of E3 ubiquitin-protein ligase UHRF1

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 UHRF1 between cysteines 333 and 363.

Details

Redox score ?
87
PDB code
3asl
Structure name
structure of uhrf1 in complex with histone tail
Structure deposition date
2010-12-16
Thiol separation (Å)
4
Half-sphere exposure sum ?
44
Minimum pKa ?
6
% buried
8
Peptide accession
Q96T88
Residue number A
333
Residue number B
363
Peptide name
E3 ubiquitin-protein ligase UHRF1

Ligandability

Cysteine 333 of E3 ubiquitin-protein ligase UHRF1

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 363 of E3 ubiquitin-protein ligase UHRF1

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 UHRF1 between cysteines 302 and 305.

Details

Redox score ?
86
PDB code
3ask
Structure name
structure of uhrf1 in complex with histone tail
Structure deposition date
2010-12-16
Thiol separation (Å)
4
Half-sphere exposure sum ?
37
Minimum pKa ?
6
% buried
5
Peptide accession
Q96T88
Residue number A
302
Residue number B
305
Peptide name
E3 ubiquitin-protein ligase UHRF1

Ligandability

Cysteine 302 of E3 ubiquitin-protein ligase UHRF1

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 305 of E3 ubiquitin-protein ligase UHRF1

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 UHRF1 between cysteines 313 and 316.

Details

Redox score ?
86
PDB code
3ask
Structure name
structure of uhrf1 in complex with histone tail
Structure deposition date
2010-12-16
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
5
% buried
14
Peptide accession
Q96T88
Residue number A
313
Residue number B
316
Peptide name
E3 ubiquitin-protein ligase UHRF1

Ligandability

Cysteine 313 of E3 ubiquitin-protein ligase UHRF1

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 316 of E3 ubiquitin-protein ligase UHRF1

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 UHRF1 between cysteines 739 and 759.

Details

Redox score ?
86
PDB code
3fl2
Structure name
crystal structure of the ring domain of the e3 ubiquitin-protein ligase uhrf1
Structure deposition date
2008-12-18
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
6
% buried
22
Peptide accession
Q96T88
Residue number A
739
Residue number B
759
Peptide name
E3 ubiquitin-protein ligase UHRF1

Ligandability

Cysteine 739 of E3 ubiquitin-protein ligase UHRF1

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 759 of E3 ubiquitin-protein ligase UHRF1

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 UHRF1 between cysteines 305 and 316 (318 and 329 respectively in this structure).

Details

Redox score ?
86
PDB code
3sou
Structure name
structure of uhrf1 phd finger in complex with histone h3 1-9 peptide
Structure deposition date
2011-06-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
5
% buried
8
Peptide accession
Q96T88
Residue number A
305
Residue number B
316
Peptide name
E3 ubiquitin-protein ligase UHRF1

Ligandability

Cysteine 305 of E3 ubiquitin-protein ligase UHRF1

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 316 of E3 ubiquitin-protein ligase UHRF1

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 UHRF1 between cysteines 305 and 313.

Details

Redox score ?
84
PDB code
3ask
Structure name
structure of uhrf1 in complex with histone tail
Structure deposition date
2010-12-16
Thiol separation (Å)
4
Half-sphere exposure sum ?
43
Minimum pKa ?
7
% buried
1
Peptide accession
Q96T88
Residue number A
305
Residue number B
313
Peptide name
E3 ubiquitin-protein ligase UHRF1

Ligandability

Cysteine 305 of E3 ubiquitin-protein ligase UHRF1

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 313 of E3 ubiquitin-protein ligase UHRF1

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 UHRF1 between cysteines 318 and 321.

Details

Redox score ?
84
PDB code
3ask
Structure name
structure of uhrf1 in complex with histone tail
Structure deposition date
2010-12-16
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
6
% buried
6
Peptide accession
Q96T88
Residue number A
318
Residue number B
321
Peptide name
E3 ubiquitin-protein ligase UHRF1

Ligandability

Cysteine 318 of E3 ubiquitin-protein ligase UHRF1

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 321 of E3 ubiquitin-protein ligase UHRF1

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 UHRF1 between cysteines 333 and 360 (346 and 373 respectively in this structure).

Details

Redox score ?
84
PDB code
3sow
Structure name
structure of uhrf1 phd finger in complex with histone h3k4me3 1-9 peptide
Structure deposition date
2011-06-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
6
% buried
34
Peptide accession
Q96T88
Residue number A
333
Residue number B
360
Peptide name
E3 ubiquitin-protein ligase UHRF1

Ligandability

Cysteine 333 of E3 ubiquitin-protein ligase UHRF1

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 360 of E3 ubiquitin-protein ligase UHRF1

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 UHRF1 between cysteines 759 and 762.

Details

Redox score ?
83
PDB code
3fl2
Structure name
crystal structure of the ring domain of the e3 ubiquitin-protein ligase uhrf1
Structure deposition date
2008-12-18
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
6
% buried
14
Peptide accession
Q96T88
Residue number A
759
Residue number B
762
Peptide name
E3 ubiquitin-protein ligase UHRF1

Ligandability

Cysteine 759 of E3 ubiquitin-protein ligase UHRF1

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 762 of E3 ubiquitin-protein ligase UHRF1

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 UHRF1 between cysteines 739 and 762.

Details

Redox score ?
81
PDB code
3fl2
Structure name
crystal structure of the ring domain of the e3 ubiquitin-protein ligase uhrf1
Structure deposition date
2008-12-18
Thiol separation (Å)
4
Half-sphere exposure sum ?
37
Minimum pKa ?
8
% buried
8
Peptide accession
Q96T88
Residue number A
739
Residue number B
762
Peptide name
E3 ubiquitin-protein ligase UHRF1

Ligandability

Cysteine 739 of E3 ubiquitin-protein ligase UHRF1

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 762 of E3 ubiquitin-protein ligase UHRF1

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 UHRF1 between cysteines 336 and 363.

Details

Redox score ?
79
PDB code
3asl
Structure name
structure of uhrf1 in complex with histone tail
Structure deposition date
2010-12-16
Thiol separation (Å)
4
Half-sphere exposure sum ?
34
Minimum pKa ?
10
% buried
6
Peptide accession
Q96T88
Residue number A
336
Residue number B
363
Peptide name
E3 ubiquitin-protein ligase UHRF1

Ligandability

Cysteine 336 of E3 ubiquitin-protein ligase UHRF1

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 363 of E3 ubiquitin-protein ligase UHRF1

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 UHRF1 between cysteines 302 and 316.

Details

Redox score ?
79
PDB code
3ask
Structure name
structure of uhrf1 in complex with histone tail
Structure deposition date
2010-12-16
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
8
% buried
18
Peptide accession
Q96T88
Residue number A
302
Residue number B
316
Peptide name
E3 ubiquitin-protein ligase UHRF1

Ligandability

Cysteine 302 of E3 ubiquitin-protein ligase UHRF1

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 316 of E3 ubiquitin-protein ligase UHRF1

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 UHRF1 between cysteines 318 and 344 (331 and 357 respectively in this structure).

Details

Redox score ?
79
PDB code
3sow
Structure name
structure of uhrf1 phd finger in complex with histone h3k4me3 1-9 peptide
Structure deposition date
2011-06-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
7
% buried
32
Peptide accession
Q96T88
Residue number A
318
Residue number B
344
Peptide name
E3 ubiquitin-protein ligase UHRF1

Ligandability

Cysteine 318 of E3 ubiquitin-protein ligase UHRF1

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 344 of E3 ubiquitin-protein ligase UHRF1

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 UHRF1 between cysteines 360 and 363 (373 and 376 respectively in this structure).

Details

Redox score ?
79
PDB code
3sow
Structure name
structure of uhrf1 phd finger in complex with histone h3k4me3 1-9 peptide
Structure deposition date
2011-06-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
9
% buried
26
Peptide accession
Q96T88
Residue number A
360
Residue number B
363
Peptide name
E3 ubiquitin-protein ligase UHRF1

Ligandability

Cysteine 360 of E3 ubiquitin-protein ligase UHRF1

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 363 of E3 ubiquitin-protein ligase UHRF1

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 UHRF1 between cysteines 727 and 747.

Details

Redox score ?
77
PDB code
3fl2
Structure name
crystal structure of the ring domain of the e3 ubiquitin-protein ligase uhrf1
Structure deposition date
2008-12-18
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
8
% buried
24
Peptide accession
Q96T88
Residue number A
727
Residue number B
747
Peptide name
E3 ubiquitin-protein ligase UHRF1

Ligandability

Cysteine 727 of E3 ubiquitin-protein ligase UHRF1

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 747 of E3 ubiquitin-protein ligase UHRF1

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 UHRF1 between cysteines 336 and 360 (349 and 373 respectively in this structure).

Details

Redox score ?
76
PDB code
3sow
Structure name
structure of uhrf1 phd finger in complex with histone h3k4me3 1-9 peptide
Structure deposition date
2011-06-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
9
% buried
38
Peptide accession
Q96T88
Residue number A
336
Residue number B
360
Peptide name
E3 ubiquitin-protein ligase UHRF1

Ligandability

Cysteine 336 of E3 ubiquitin-protein ligase UHRF1

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 360 of E3 ubiquitin-protein ligase UHRF1

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 UHRF1 between cysteines 727 and 744.

Details

Redox score ?
76
PDB code
3fl2
Structure name
crystal structure of the ring domain of the e3 ubiquitin-protein ligase uhrf1
Structure deposition date
2008-12-18
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
8
% buried
36
Peptide accession
Q96T88
Residue number A
727
Residue number B
744
Peptide name
E3 ubiquitin-protein ligase UHRF1

Ligandability

Cysteine 727 of E3 ubiquitin-protein ligase UHRF1

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 744 of E3 ubiquitin-protein ligase UHRF1

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 UHRF1 between cysteines 321 and 344 (334 and 357 respectively in this structure).

Details

Redox score ?
75
PDB code
3sou
Structure name
structure of uhrf1 phd finger in complex with histone h3 1-9 peptide
Structure deposition date
2011-06-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
9
% buried
16
Peptide accession
Q96T88
Residue number A
321
Residue number B
344
Peptide name
E3 ubiquitin-protein ligase UHRF1

Ligandability

Cysteine 321 of E3 ubiquitin-protein ligase UHRF1

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 344 of E3 ubiquitin-protein ligase UHRF1

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 UHRF1 between cysteines 744 and 747.

Details

Redox score ?
68
PDB code
3fl2
Structure name
crystal structure of the ring domain of the e3 ubiquitin-protein ligase uhrf1
Structure deposition date
2008-12-18
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
10
% buried
41
Peptide accession
Q96T88
Residue number A
744
Residue number B
747
Peptide name
E3 ubiquitin-protein ligase UHRF1

Ligandability

Cysteine 744 of E3 ubiquitin-protein ligase UHRF1

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 747 of E3 ubiquitin-protein ligase UHRF1

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 UHRF1 between cysteines 726 and 747.

Details

Redox score ?
66
PDB code
3fl2
Structure name
crystal structure of the ring domain of the e3 ubiquitin-protein ligase uhrf1
Structure deposition date
2008-12-18
Thiol separation (Å)
5
Half-sphere exposure sum ?
56
Minimum pKa ?
10
% buried
31
Peptide accession
Q96T88
Residue number A
726
Residue number B
747
Peptide name
E3 ubiquitin-protein ligase UHRF1

Ligandability

Cysteine 726 of E3 ubiquitin-protein ligase UHRF1

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 747 of E3 ubiquitin-protein ligase UHRF1

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 UHRF1 between cysteines 726 and 727.

Details

Redox score ?
62
PDB code
3fl2
Structure name
crystal structure of the ring domain of the e3 ubiquitin-protein ligase uhrf1
Structure deposition date
2008-12-18
Thiol separation (Å)
7
Half-sphere exposure sum ?
47
Minimum pKa ?
8
% buried
26
Peptide accession
Q96T88
Residue number A
726
Residue number B
727
Peptide name
E3 ubiquitin-protein ligase UHRF1

Ligandability

Cysteine 726 of E3 ubiquitin-protein ligase UHRF1

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 727 of E3 ubiquitin-protein ligase UHRF1

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 UHRF1 between cysteines 240 and 266. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
59
PDB code
6vee
Structure name
solution structure of the ttd and linker region of mouse uhrf1 (np95)
Structure deposition date
2019-12-31
Thiol separation (Å)
7
Half-sphere exposure sum ?
46
Minimum pKa ?
9
% buried
19
Peptide accession
Q8VDF2
Residue number A
240
Residue number B
266
Peptide name
E3 ubiquitin-protein ligase UHRF1

Ligandability

Cysteine 240 of E3 ubiquitin-protein ligase UHRF1

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 266 of E3 ubiquitin-protein ligase UHRF1

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 UHRF1 between cysteines 726 and 759. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
3fl2
Structure name
crystal structure of the ring domain of the e3 ubiquitin-protein ligase uhrf1
Structure deposition date
2008-12-18
Thiol separation (Å)
8
Half-sphere exposure sum ?
57
Minimum pKa ?
6
% buried
30
Peptide accession
Q96T88
Residue number A
726
Residue number B
759
Peptide name
E3 ubiquitin-protein ligase UHRF1

Ligandability

Cysteine 726 of E3 ubiquitin-protein ligase UHRF1

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 759 of E3 ubiquitin-protein ligase UHRF1

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 UHRF1 between cysteines 724 and 759. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
3fl2
Structure name
crystal structure of the ring domain of the e3 ubiquitin-protein ligase uhrf1
Structure deposition date
2008-12-18
Thiol separation (Å)
10
Half-sphere exposure sum ?
60
Minimum pKa ?
3
% buried
40
Peptide accession
Q96T88
Residue number A
724
Residue number B
759
Peptide name
E3 ubiquitin-protein ligase UHRF1

Ligandability

Cysteine 724 of E3 ubiquitin-protein ligase UHRF1

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 759 of E3 ubiquitin-protein ligase UHRF1

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 UHRF1 between cysteines 318 and 360. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
3ask
Structure name
structure of uhrf1 in complex with histone tail
Structure deposition date
2010-12-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
53
Minimum pKa ?
9
% buried
12
Peptide accession
Q96T88
Residue number A
318
Residue number B
360
Peptide name
E3 ubiquitin-protein ligase UHRF1

Ligandability

Cysteine 318 of E3 ubiquitin-protein ligase UHRF1

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 360 of E3 ubiquitin-protein ligase UHRF1

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 UHRF1 between cysteines 726 and 744. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
3fl2
Structure name
crystal structure of the ring domain of the e3 ubiquitin-protein ligase uhrf1
Structure deposition date
2008-12-18
Thiol separation (Å)
7
Half-sphere exposure sum ?
62
Minimum pKa ?
11
% buried
43
Peptide accession
Q96T88
Residue number A
726
Residue number B
744
Peptide name
E3 ubiquitin-protein ligase UHRF1

Ligandability

Cysteine 726 of E3 ubiquitin-protein ligase UHRF1

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 744 of E3 ubiquitin-protein ligase UHRF1

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 UHRF1 between cysteines 313 and 321 (326 and 334 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
2lgl
Structure name
nmr structure of the uhrf1 phd domain
Structure deposition date
2011-07-28
Thiol separation (Å)
10
Half-sphere exposure sum ?
53
Minimum pKa ?
8
% buried
2
Peptide accession
Q96T88
Residue number A
313
Residue number B
321
Peptide name
E3 ubiquitin-protein ligase UHRF1

Ligandability

Cysteine 313 of E3 ubiquitin-protein ligase UHRF1

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 321 of E3 ubiquitin-protein ligase UHRF1

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 UHRF1 between cysteines 313 and 318 (326 and 331 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
2lgg
Structure name
structure of phd domain of uhrf1 in complex with h3 peptide
Structure deposition date
2011-07-26
Thiol separation (Å)
10
Half-sphere exposure sum ?
64
Minimum pKa ?
7
% buried
21
Peptide accession
Q96T88
Residue number A
313
Residue number B
318
Peptide name
E3 ubiquitin-protein ligase UHRF1

Ligandability

Cysteine 313 of E3 ubiquitin-protein ligase UHRF1

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 318 of E3 ubiquitin-protein ligase UHRF1

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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