ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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E3 ubiquitin-protein ligase COP1

Intramolecular
Cysteine 559 and cysteine 560
Cysteine 559 and cysteine 575
Cysteine 433 and cysteine 704
Cysteine 475 and cysteine 516
Cysteine 575 and cysteine 579
Cysteine 560 and cysteine 575
Cysteine 475 and cysteine 704
Cysteine 475 and cysteine 560
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase COP1 between cysteines 559 and 560. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
5hqg
Structure name
wd40 domain of human e3 ubiquitin ligase cop1 (rfwd2)
Structure deposition date
2016-01-21
Thiol separation (Å)
6
Half-sphere exposure sum ?
93
Minimum pKa ?
11
% buried
92
Peptide accession
Q8NHY2
Residue number A
559
Residue number B
560
Peptide name
E3 ubiquitin-protein ligase COP1

Ligandability

Cysteine 559 of E3 ubiquitin-protein ligase COP1

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 560 of E3 ubiquitin-protein ligase COP1

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 COP1 between cysteines 559 and 575. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
5hqg
Structure name
wd40 domain of human e3 ubiquitin ligase cop1 (rfwd2)
Structure deposition date
2016-01-21
Thiol separation (Å)
7
Half-sphere exposure sum ?
86
Minimum pKa ?
11
% buried
72
Peptide accession
Q8NHY2
Residue number A
559
Residue number B
575
Peptide name
E3 ubiquitin-protein ligase COP1

Ligandability

Cysteine 559 of E3 ubiquitin-protein ligase COP1

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 575 of E3 ubiquitin-protein ligase COP1

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 COP1 between cysteines 433 and 704. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
5igq
Structure name
wd40 domain of human e3 ubiquitin ligase cop1 (rfwd2) bound to peptide from trib1
Structure deposition date
2016-02-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
74
Minimum pKa ?
11
% buried
71
Peptide accession
Q8NHY2
Residue number A
433
Residue number B
704
Peptide name
E3 ubiquitin-protein ligase COP1

Ligandability

Cysteine 433 of E3 ubiquitin-protein ligase COP1

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 704 of E3 ubiquitin-protein ligase COP1

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 COP1 between cysteines 475 and 516. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
5igq
Structure name
wd40 domain of human e3 ubiquitin ligase cop1 (rfwd2) bound to peptide from trib1
Structure deposition date
2016-02-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
94
Minimum pKa ?
9
% buried
100
Peptide accession
Q8NHY2
Residue number A
475
Residue number B
516
Peptide name
E3 ubiquitin-protein ligase COP1

Ligandability

Cysteine 475 of E3 ubiquitin-protein ligase COP1

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 516 of E3 ubiquitin-protein ligase COP1

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 COP1 between cysteines 575 and 579. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
5igq
Structure name
wd40 domain of human e3 ubiquitin ligase cop1 (rfwd2) bound to peptide from trib1
Structure deposition date
2016-02-28
Thiol separation (Å)
8
Half-sphere exposure sum ?
85
Minimum pKa ?
13
% buried
98
Peptide accession
Q8NHY2
Residue number A
575
Residue number B
579
Peptide name
E3 ubiquitin-protein ligase COP1

Ligandability

Cysteine 575 of E3 ubiquitin-protein ligase COP1

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 579 of E3 ubiquitin-protein ligase COP1

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 COP1 between cysteines 560 and 575. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
29
PDB code
5igq
Structure name
wd40 domain of human e3 ubiquitin ligase cop1 (rfwd2) bound to peptide from trib1
Structure deposition date
2016-02-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
96
Minimum pKa ?
11
% buried
87
Peptide accession
Q8NHY2
Residue number A
560
Residue number B
575
Peptide name
E3 ubiquitin-protein ligase COP1

Ligandability

Cysteine 560 of E3 ubiquitin-protein ligase COP1

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 575 of E3 ubiquitin-protein ligase COP1

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 COP1 between cysteines 475 and 704. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
27
PDB code
5igq
Structure name
wd40 domain of human e3 ubiquitin ligase cop1 (rfwd2) bound to peptide from trib1
Structure deposition date
2016-02-28
Thiol separation (Å)
10
Half-sphere exposure sum ?
96
Minimum pKa ?
10
% buried
100
Peptide accession
Q8NHY2
Residue number A
475
Residue number B
704
Peptide name
E3 ubiquitin-protein ligase COP1

Ligandability

Cysteine 475 of E3 ubiquitin-protein ligase COP1

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 704 of E3 ubiquitin-protein ligase COP1

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 COP1 between cysteines 475 and 560. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
26
PDB code
5hqg
Structure name
wd40 domain of human e3 ubiquitin ligase cop1 (rfwd2)
Structure deposition date
2016-01-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
99
Minimum pKa ?
11
% buried
100
Peptide accession
Q8NHY2
Residue number A
475
Residue number B
560
Peptide name
E3 ubiquitin-protein ligase COP1

Ligandability

Cysteine 475 of E3 ubiquitin-protein ligase COP1

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 560 of E3 ubiquitin-protein ligase COP1

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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