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E3 ubiquitin-protein ligase RNF213

Intramolecular
Cysteine 3982 and cysteine 3985
Cysteine 3962 and cysteine 3985
Cysteine 951 and cysteine 992
Cysteine 3962 and cysteine 3982
Cysteine 3947 and cysteine 3950
Cysteine 3947 and cysteine 3970
Cysteine 3947 and cysteine 3967
Cysteine 2605 and cysteine 2653
Cysteine 3950 and cysteine 3967
Cysteine 618 and cysteine 656
More...
Cysteine 3967 and cysteine 3970
Cysteine 3950 and cysteine 3970
Cysteine 1710 and cysteine 1767
Cysteine 2190 and cysteine 2196
Cysteine 2185 and cysteine 2373
Cysteine 1892 and cysteine 1899
Cysteine 3947 and cysteine 3982
Cysteine 653 and cysteine 656
Cysteine 618 and cysteine 653
Cysteine 4799 and cysteine 4800
Cysteine 1607 and cysteine 1608
Cysteine 2574 and cysteine 2671
Cysteine 3931 and cysteine 4015
Cysteine 656 and cysteine 661
Cysteine 4799 and cysteine 4822
Cysteine 1698 and cysteine 1767
Cysteine 951 and cysteine 955
Cysteine 955 and cysteine 992
Cysteine 955 and cysteine 971
Cysteine 3959 and cysteine 3962
Cysteine 1797 and cysteine 1892
Cysteine 3929 and cysteine 3931
Cysteine 3740 and cysteine 3853
Cysteine 2653 and cysteine 2719
Cysteine 1843 and cysteine 1878
Cysteine 1827 and cysteine 1892
Cysteine 3929 and cysteine 4015
Cysteine 4127 and cysteine 4880
Cysteine 2786 and cysteine 2829
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF213 between cysteines 3982 and 3985.

Details

Redox score ?
90
PDB code
6tay
Structure name
mouse rnf213 mutant r4753k modeling the moyamoya-disease-related human variant r4810k
Structure deposition date
2019-10-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
41
Minimum pKa ?
5
% buried
12
Peptide accession
E9Q555
Residue number A
3982
Residue number B
3985
Peptide name
E3 ubiquitin-protein ligase RNF213

Ligandability

Cysteine 3982 of E3 ubiquitin-protein ligase RNF213

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 3985 of E3 ubiquitin-protein ligase RNF213

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 RNF213 between cysteines 3962 and 3985.

Details

Redox score ?
87
PDB code
6tax
Structure name
mouse rnf213 wild type protein
Structure deposition date
2019-10-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
34
Minimum pKa ?
6
% buried
8
Peptide accession
E9Q555
Residue number A
3962
Residue number B
3985
Peptide name
E3 ubiquitin-protein ligase RNF213

Ligandability

Cysteine 3962 of E3 ubiquitin-protein ligase RNF213

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 3985 of E3 ubiquitin-protein ligase RNF213

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 RNF213 between cysteines 951 and 992.

Details

Redox score ?
87
PDB code
7oik
Structure name
mouse rnf213:ube2l3 transthiolation intermediate, chemically stabilized
Structure deposition date
2021-05-11
Thiol separation (Å)
2
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
E9Q555
Residue number A
951
Residue number B
992
Peptide name
E3 ubiquitin-protein ligase RNF213

Ligandability

Cysteine 951 of E3 ubiquitin-protein ligase RNF213

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 992 of E3 ubiquitin-protein ligase RNF213

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 RNF213 between cysteines 3962 and 3982.

Details

Redox score ?
86
PDB code
6tay
Structure name
mouse rnf213 mutant r4753k modeling the moyamoya-disease-related human variant r4810k
Structure deposition date
2019-10-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
44
Minimum pKa ?
5
% buried
22
Peptide accession
E9Q555
Residue number A
3962
Residue number B
3982
Peptide name
E3 ubiquitin-protein ligase RNF213

Ligandability

Cysteine 3962 of E3 ubiquitin-protein ligase RNF213

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 3982 of E3 ubiquitin-protein ligase RNF213

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 RNF213 between cysteines 3947 and 3950.

Details

Redox score ?
83
PDB code
7oim
Structure name
mouse rnf213, with mixed nucleotides bound
Structure deposition date
2021-05-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
4
% buried
52
Peptide accession
E9Q555
Residue number A
3947
Residue number B
3950
Peptide name
E3 ubiquitin-protein ligase RNF213

Ligandability

Cysteine 3947 of E3 ubiquitin-protein ligase RNF213

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 3950 of E3 ubiquitin-protein ligase RNF213

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 RNF213 between cysteines 3947 and 3970.

Details

Redox score ?
83
PDB code
7oim
Structure name
mouse rnf213, with mixed nucleotides bound
Structure deposition date
2021-05-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
4
% buried
40
Peptide accession
E9Q555
Residue number A
3947
Residue number B
3970
Peptide name
E3 ubiquitin-protein ligase RNF213

Ligandability

Cysteine 3947 of E3 ubiquitin-protein ligase RNF213

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 3970 of E3 ubiquitin-protein ligase RNF213

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 RNF213 between cysteines 3947 and 3967.

Details

Redox score ?
82
PDB code
7oim
Structure name
mouse rnf213, with mixed nucleotides bound
Structure deposition date
2021-05-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
4
% buried
49
Peptide accession
E9Q555
Residue number A
3947
Residue number B
3967
Peptide name
E3 ubiquitin-protein ligase RNF213

Ligandability

Cysteine 3947 of E3 ubiquitin-protein ligase RNF213

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 3967 of E3 ubiquitin-protein ligase RNF213

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 RNF213 between cysteines 2605 and 2653.

Details

Redox score ?
81
PDB code
6tax
Structure name
mouse rnf213 wild type protein
Structure deposition date
2019-10-31
Thiol separation (Å)
2
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
E9Q555
Residue number A
2605
Residue number B
2653
Peptide name
E3 ubiquitin-protein ligase RNF213

Ligandability

Cysteine 2605 of E3 ubiquitin-protein ligase RNF213

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 2653 of E3 ubiquitin-protein ligase RNF213

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 RNF213 between cysteines 3950 and 3967.

Details

Redox score ?
80
PDB code
7oim
Structure name
mouse rnf213, with mixed nucleotides bound
Structure deposition date
2021-05-11
Thiol separation (Å)
3
Half-sphere exposure sum ?
57
Minimum pKa ?
8
% buried
42
Peptide accession
E9Q555
Residue number A
3950
Residue number B
3967
Peptide name
E3 ubiquitin-protein ligase RNF213

Ligandability

Cysteine 3950 of E3 ubiquitin-protein ligase RNF213

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 3967 of E3 ubiquitin-protein ligase RNF213

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 RNF213 between cysteines 618 and 656.

Details

Redox score ?
75
PDB code
6tay
Structure name
mouse rnf213 mutant r4753k modeling the moyamoya-disease-related human variant r4810k
Structure deposition date
2019-10-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
8
% buried
84
Peptide accession
E9Q555
Residue number A
618
Residue number B
656
Peptide name
E3 ubiquitin-protein ligase RNF213

Ligandability

Cysteine 618 of E3 ubiquitin-protein ligase RNF213

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 656 of E3 ubiquitin-protein ligase RNF213

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 RNF213 between cysteines 3967 and 3970.

Details

Redox score ?
74
PDB code
6tax
Structure name
mouse rnf213 wild type protein
Structure deposition date
2019-10-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
8
% buried
33
Peptide accession
E9Q555
Residue number A
3967
Residue number B
3970
Peptide name
E3 ubiquitin-protein ligase RNF213

Ligandability

Cysteine 3967 of E3 ubiquitin-protein ligase RNF213

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 3970 of E3 ubiquitin-protein ligase RNF213

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 RNF213 between cysteines 3950 and 3970.

Details

Redox score ?
71
PDB code
6tay
Structure name
mouse rnf213 mutant r4753k modeling the moyamoya-disease-related human variant r4810k
Structure deposition date
2019-10-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
9
% buried
34
Peptide accession
E9Q555
Residue number A
3950
Residue number B
3970
Peptide name
E3 ubiquitin-protein ligase RNF213

Ligandability

Cysteine 3950 of E3 ubiquitin-protein ligase RNF213

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 3970 of E3 ubiquitin-protein ligase RNF213

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 RNF213 between cysteines 1710 and 1767. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
59
PDB code
7oik
Structure name
mouse rnf213:ube2l3 transthiolation intermediate, chemically stabilized
Structure deposition date
2021-05-11
Thiol separation (Å)
6
Half-sphere exposure sum ?
61
Minimum pKa ?
10
% buried
54
Peptide accession
E9Q555
Residue number A
1710
Residue number B
1767
Peptide name
E3 ubiquitin-protein ligase RNF213

Ligandability

Cysteine 1710 of E3 ubiquitin-protein ligase RNF213

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 1767 of E3 ubiquitin-protein ligase RNF213

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 RNF213 between cysteines 2190 and 2196. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
59
PDB code
7oim
Structure name
mouse rnf213, with mixed nucleotides bound
Structure deposition date
2021-05-11
Thiol separation (Å)
7
Half-sphere exposure sum ?
57
Minimum pKa ?
9
% buried
58
Peptide accession
E9Q555
Residue number A
2190
Residue number B
2196
Peptide name
E3 ubiquitin-protein ligase RNF213

Ligandability

Cysteine 2190 of E3 ubiquitin-protein ligase RNF213

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 2196 of E3 ubiquitin-protein ligase RNF213

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 RNF213 between cysteines 2185 and 2373. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
7oim
Structure name
mouse rnf213, with mixed nucleotides bound
Structure deposition date
2021-05-11
Thiol separation (Å)
5
Half-sphere exposure sum ?
59
Minimum pKa ?
11
% buried
84
Peptide accession
E9Q555
Residue number A
2185
Residue number B
2373
Peptide name
E3 ubiquitin-protein ligase RNF213

Ligandability

Cysteine 2185 of E3 ubiquitin-protein ligase RNF213

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 2373 of E3 ubiquitin-protein ligase RNF213

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 RNF213 between cysteines 1892 and 1899. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
7oim
Structure name
mouse rnf213, with mixed nucleotides bound
Structure deposition date
2021-05-11
Thiol separation (Å)
7
Half-sphere exposure sum ?
65
Minimum pKa ?
10
% buried
54
Peptide accession
E9Q555
Residue number A
1892
Residue number B
1899
Peptide name
E3 ubiquitin-protein ligase RNF213

Ligandability

Cysteine 1892 of E3 ubiquitin-protein ligase RNF213

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 1899 of E3 ubiquitin-protein ligase RNF213

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 RNF213 between cysteines 3947 and 3982. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
7oim
Structure name
mouse rnf213, with mixed nucleotides bound
Structure deposition date
2021-05-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
60
Minimum pKa ?
4
% buried
42
Peptide accession
E9Q555
Residue number A
3947
Residue number B
3982
Peptide name
E3 ubiquitin-protein ligase RNF213

Ligandability

Cysteine 3947 of E3 ubiquitin-protein ligase RNF213

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 3982 of E3 ubiquitin-protein ligase RNF213

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 RNF213 between cysteines 653 and 656. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
6tax
Structure name
mouse rnf213 wild type protein
Structure deposition date
2019-10-31
Thiol separation (Å)
6
Half-sphere exposure sum ?
64
Minimum pKa ?
13
% buried
88
Peptide accession
E9Q555
Residue number A
653
Residue number B
656
Peptide name
E3 ubiquitin-protein ligase RNF213

Ligandability

Cysteine 653 of E3 ubiquitin-protein ligase RNF213

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 656 of E3 ubiquitin-protein ligase RNF213

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 RNF213 between cysteines 618 and 653. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
6tay
Structure name
mouse rnf213 mutant r4753k modeling the moyamoya-disease-related human variant r4810k
Structure deposition date
2019-10-31
Thiol separation (Å)
7
Half-sphere exposure sum ?
72
Minimum pKa ?
8
% buried
94
Peptide accession
E9Q555
Residue number A
618
Residue number B
653
Peptide name
E3 ubiquitin-protein ligase RNF213

Ligandability

Cysteine 618 of E3 ubiquitin-protein ligase RNF213

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 653 of E3 ubiquitin-protein ligase RNF213

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 RNF213 between cysteines 4799 and 4800. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
6tay
Structure name
mouse rnf213 mutant r4753k modeling the moyamoya-disease-related human variant r4810k
Structure deposition date
2019-10-31
Thiol separation (Å)
8
Half-sphere exposure sum ?
56
Minimum pKa ?
10
% buried
38
Peptide accession
E9Q555
Residue number A
4799
Residue number B
4800
Peptide name
E3 ubiquitin-protein ligase RNF213

Ligandability

Cysteine 4799 of E3 ubiquitin-protein ligase RNF213

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 4800 of E3 ubiquitin-protein ligase RNF213

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 RNF213 between cysteines 1607 and 1608. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
7oim
Structure name
mouse rnf213, with mixed nucleotides bound
Structure deposition date
2021-05-11
Thiol separation (Å)
7
Half-sphere exposure sum ?
67
Minimum pKa ?
10
% buried
46
Peptide accession
E9Q555
Residue number A
1607
Residue number B
1608
Peptide name
E3 ubiquitin-protein ligase RNF213

Ligandability

Cysteine 1607 of E3 ubiquitin-protein ligase RNF213

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 1608 of E3 ubiquitin-protein ligase RNF213

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 RNF213 between cysteines 2574 and 2671. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
7oik
Structure name
mouse rnf213:ube2l3 transthiolation intermediate, chemically stabilized
Structure deposition date
2021-05-11
Thiol separation (Å)
8
Half-sphere exposure sum ?
55
Minimum pKa ?
10
% buried
21
Peptide accession
E9Q555
Residue number A
2574
Residue number B
2671
Peptide name
E3 ubiquitin-protein ligase RNF213

Ligandability

Cysteine 2574 of E3 ubiquitin-protein ligase RNF213

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 2671 of E3 ubiquitin-protein ligase RNF213

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 RNF213 between cysteines 3931 and 4015. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
7oik
Structure name
mouse rnf213:ube2l3 transthiolation intermediate, chemically stabilized
Structure deposition date
2021-05-11
Thiol separation (Å)
7
Half-sphere exposure sum ?
64
Minimum pKa ?
12
% buried
88
Peptide accession
E9Q555
Residue number A
3931
Residue number B
4015
Peptide name
E3 ubiquitin-protein ligase RNF213

Ligandability

Cysteine 3931 of E3 ubiquitin-protein ligase RNF213

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 4015 of E3 ubiquitin-protein ligase RNF213

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 RNF213 between cysteines 656 and 661. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
6tay
Structure name
mouse rnf213 mutant r4753k modeling the moyamoya-disease-related human variant r4810k
Structure deposition date
2019-10-31
Thiol separation (Å)
8
Half-sphere exposure sum ?
58
Minimum pKa ?
11
% buried
66
Peptide accession
E9Q555
Residue number A
656
Residue number B
661
Peptide name
E3 ubiquitin-protein ligase RNF213

Ligandability

Cysteine 656 of E3 ubiquitin-protein ligase RNF213

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 661 of E3 ubiquitin-protein ligase RNF213

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 RNF213 between cysteines 4799 and 4822. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
6tax
Structure name
mouse rnf213 wild type protein
Structure deposition date
2019-10-31
Thiol separation (Å)
8
Half-sphere exposure sum ?
74
Minimum pKa ?
12
% buried
68
Peptide accession
E9Q555
Residue number A
4799
Residue number B
4822
Peptide name
E3 ubiquitin-protein ligase RNF213

Ligandability

Cysteine 4799 of E3 ubiquitin-protein ligase RNF213

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 4822 of E3 ubiquitin-protein ligase RNF213

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 RNF213 between cysteines 1698 and 1767. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
7oik
Structure name
mouse rnf213:ube2l3 transthiolation intermediate, chemically stabilized
Structure deposition date
2021-05-11
Thiol separation (Å)
8
Half-sphere exposure sum ?
62
Minimum pKa ?
11
% buried
66
Peptide accession
E9Q555
Residue number A
1698
Residue number B
1767
Peptide name
E3 ubiquitin-protein ligase RNF213

Ligandability

Cysteine 1698 of E3 ubiquitin-protein ligase RNF213

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 1767 of E3 ubiquitin-protein ligase RNF213

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 RNF213 between cysteines 951 and 955. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
6tay
Structure name
mouse rnf213 mutant r4753k modeling the moyamoya-disease-related human variant r4810k
Structure deposition date
2019-10-31
Thiol separation (Å)
8
Half-sphere exposure sum ?
65
Minimum pKa ?
12
% buried
nan
Peptide accession
E9Q555
Residue number A
951
Residue number B
955
Peptide name
E3 ubiquitin-protein ligase RNF213

Ligandability

Cysteine 951 of E3 ubiquitin-protein ligase RNF213

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 955 of E3 ubiquitin-protein ligase RNF213

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 RNF213 between cysteines 955 and 992. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
7oik
Structure name
mouse rnf213:ube2l3 transthiolation intermediate, chemically stabilized
Structure deposition date
2021-05-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
58
Minimum pKa ?
11
% buried
nan
Peptide accession
E9Q555
Residue number A
955
Residue number B
992
Peptide name
E3 ubiquitin-protein ligase RNF213

Ligandability

Cysteine 955 of E3 ubiquitin-protein ligase RNF213

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 992 of E3 ubiquitin-protein ligase RNF213

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 RNF213 between cysteines 955 and 971. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
7oim
Structure name
mouse rnf213, with mixed nucleotides bound
Structure deposition date
2021-05-11
Thiol separation (Å)
8
Half-sphere exposure sum ?
63
Minimum pKa ?
11
% buried
79
Peptide accession
E9Q555
Residue number A
955
Residue number B
971
Peptide name
E3 ubiquitin-protein ligase RNF213

Ligandability

Cysteine 955 of E3 ubiquitin-protein ligase RNF213

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 971 of E3 ubiquitin-protein ligase RNF213

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 RNF213 between cysteines 3959 and 3962. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
7oik
Structure name
mouse rnf213:ube2l3 transthiolation intermediate, chemically stabilized
Structure deposition date
2021-05-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
50
Minimum pKa ?
10
% buried
20
Peptide accession
E9Q555
Residue number A
3959
Residue number B
3962
Peptide name
E3 ubiquitin-protein ligase RNF213

Ligandability

Cysteine 3959 of E3 ubiquitin-protein ligase RNF213

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 3962 of E3 ubiquitin-protein ligase RNF213

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 RNF213 between cysteines 1797 and 1892. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
6tax
Structure name
mouse rnf213 wild type protein
Structure deposition date
2019-10-31
Thiol separation (Å)
8
Half-sphere exposure sum ?
75
Minimum pKa ?
12
% buried
80
Peptide accession
E9Q555
Residue number A
1797
Residue number B
1892
Peptide name
E3 ubiquitin-protein ligase RNF213

Ligandability

Cysteine 1797 of E3 ubiquitin-protein ligase RNF213

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 1892 of E3 ubiquitin-protein ligase RNF213

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 RNF213 between cysteines 3929 and 3931. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
7oik
Structure name
mouse rnf213:ube2l3 transthiolation intermediate, chemically stabilized
Structure deposition date
2021-05-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
54
Minimum pKa ?
10
% buried
54
Peptide accession
E9Q555
Residue number A
3929
Residue number B
3931
Peptide name
E3 ubiquitin-protein ligase RNF213

Ligandability

Cysteine 3929 of E3 ubiquitin-protein ligase RNF213

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 3931 of E3 ubiquitin-protein ligase RNF213

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 RNF213 between cysteines 3740 and 3853. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
6tay
Structure name
mouse rnf213 mutant r4753k modeling the moyamoya-disease-related human variant r4810k
Structure deposition date
2019-10-31
Thiol separation (Å)
9
Half-sphere exposure sum ?
57
Minimum pKa ?
10
% buried
66
Peptide accession
E9Q555
Residue number A
3740
Residue number B
3853
Peptide name
E3 ubiquitin-protein ligase RNF213

Ligandability

Cysteine 3740 of E3 ubiquitin-protein ligase RNF213

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 3853 of E3 ubiquitin-protein ligase RNF213

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 RNF213 between cysteines 2653 and 2719. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
7oik
Structure name
mouse rnf213:ube2l3 transthiolation intermediate, chemically stabilized
Structure deposition date
2021-05-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
12
% buried
nan
Peptide accession
E9Q555
Residue number A
2653
Residue number B
2719
Peptide name
E3 ubiquitin-protein ligase RNF213

Ligandability

Cysteine 2653 of E3 ubiquitin-protein ligase RNF213

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 2719 of E3 ubiquitin-protein ligase RNF213

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 RNF213 between cysteines 1843 and 1878. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
7oim
Structure name
mouse rnf213, with mixed nucleotides bound
Structure deposition date
2021-05-11
Thiol separation (Å)
8
Half-sphere exposure sum ?
72
Minimum pKa ?
12
% buried
88
Peptide accession
E9Q555
Residue number A
1843
Residue number B
1878
Peptide name
E3 ubiquitin-protein ligase RNF213

Ligandability

Cysteine 1843 of E3 ubiquitin-protein ligase RNF213

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 1878 of E3 ubiquitin-protein ligase RNF213

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 RNF213 between cysteines 1827 and 1892. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
7oik
Structure name
mouse rnf213:ube2l3 transthiolation intermediate, chemically stabilized
Structure deposition date
2021-05-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
13
% buried
92
Peptide accession
E9Q555
Residue number A
1827
Residue number B
1892
Peptide name
E3 ubiquitin-protein ligase RNF213

Ligandability

Cysteine 1827 of E3 ubiquitin-protein ligase RNF213

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 1892 of E3 ubiquitin-protein ligase RNF213

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 RNF213 between cysteines 3929 and 4015. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
6tay
Structure name
mouse rnf213 mutant r4753k modeling the moyamoya-disease-related human variant r4810k
Structure deposition date
2019-10-31
Thiol separation (Å)
9
Half-sphere exposure sum ?
67
Minimum pKa ?
11
% buried
83
Peptide accession
E9Q555
Residue number A
3929
Residue number B
4015
Peptide name
E3 ubiquitin-protein ligase RNF213

Ligandability

Cysteine 3929 of E3 ubiquitin-protein ligase RNF213

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 4015 of E3 ubiquitin-protein ligase RNF213

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 RNF213 between cysteines 4127 and 4880. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
6tay
Structure name
mouse rnf213 mutant r4753k modeling the moyamoya-disease-related human variant r4810k
Structure deposition date
2019-10-31
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
11
% buried
94
Peptide accession
E9Q555
Residue number A
4127
Residue number B
4880
Peptide name
E3 ubiquitin-protein ligase RNF213

Ligandability

Cysteine 4127 of E3 ubiquitin-protein ligase RNF213

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 4880 of E3 ubiquitin-protein ligase RNF213

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 RNF213 between cysteines 2786 and 2829. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
7oim
Structure name
mouse rnf213, with mixed nucleotides bound
Structure deposition date
2021-05-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
67
Minimum pKa ?
10
% buried
57
Peptide accession
E9Q555
Residue number A
2786
Residue number B
2829
Peptide name
E3 ubiquitin-protein ligase RNF213

Ligandability

Cysteine 2786 of E3 ubiquitin-protein ligase RNF213

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 2829 of E3 ubiquitin-protein ligase RNF213

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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