ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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E3 ubiquitin-protein ligase RNF38

Intramolecular
Cysteine 481 and cysteine 503
Cysteine 466 and cysteine 468
Cysteine 463 and cysteine 466
Cysteine 466 and cysteine 489
Cysteine 481 and cysteine 500
Cysteine 463 and cysteine 489
Cysteine 463 and cysteine 468
Cysteine 500 and cysteine 503
Cysteine 468 and cysteine 489
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF38 between cysteines 481 and 503 (431 and 453 respectively in this structure).

Details

Redox score ?
76
PDB code
7ojx
Structure name
e2 ube2k covalently linked to donor ub, acceptor di-ub, and ring e3 primed for k48-linked ub chain synthesis
Structure deposition date
2021-05-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
7
% buried
60
Peptide accession
Q9H0F5
Residue number A
481
Residue number B
503
Peptide name
E3 ubiquitin-protein ligase RNF38

Ligandability

Cysteine 481 of E3 ubiquitin-protein ligase RNF38

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 503 of E3 ubiquitin-protein ligase RNF38

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 RNF38 between cysteines 466 and 468 (416 and 418 respectively in this structure).

Details

Redox score ?
74
PDB code
4v3l
Structure name
rnf38-ub-ubch5b-ub complex
Structure deposition date
2014-10-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
8
% buried
42
Peptide accession
Q9H0F5
Residue number A
466
Residue number B
468
Peptide name
E3 ubiquitin-protein ligase RNF38

Ligandability

Cysteine 466 of E3 ubiquitin-protein ligase RNF38

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 468 of E3 ubiquitin-protein ligase RNF38

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 RNF38 between cysteines 463 and 466 (413 and 416 respectively in this structure).

Details

Redox score ?
72
PDB code
7ojx
Structure name
e2 ube2k covalently linked to donor ub, acceptor di-ub, and ring e3 primed for k48-linked ub chain synthesis
Structure deposition date
2021-05-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
73
Minimum pKa ?
8
% buried
nan
Peptide accession
Q9H0F5
Residue number A
463
Residue number B
466
Peptide name
E3 ubiquitin-protein ligase RNF38

Ligandability

Cysteine 463 of E3 ubiquitin-protein ligase RNF38

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 466 of E3 ubiquitin-protein ligase RNF38

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 RNF38 between cysteines 466 and 489 (416 and 439 respectively in this structure).

Details

Redox score ?
67
PDB code
4v3l
Structure name
rnf38-ub-ubch5b-ub complex
Structure deposition date
2014-10-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
10
% buried
60
Peptide accession
Q9H0F5
Residue number A
466
Residue number B
489
Peptide name
E3 ubiquitin-protein ligase RNF38

Ligandability

Cysteine 466 of E3 ubiquitin-protein ligase RNF38

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 489 of E3 ubiquitin-protein ligase RNF38

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 RNF38 between cysteines 481 and 500 (431 and 450 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
7ojx
Structure name
e2 ube2k covalently linked to donor ub, acceptor di-ub, and ring e3 primed for k48-linked ub chain synthesis
Structure deposition date
2021-05-17
Thiol separation (Å)
3
Half-sphere exposure sum ?
66
Minimum pKa ?
18
% buried
nan
Peptide accession
Q9H0F5
Residue number A
481
Residue number B
500
Peptide name
E3 ubiquitin-protein ligase RNF38

Ligandability

Cysteine 481 of E3 ubiquitin-protein ligase RNF38

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 500 of E3 ubiquitin-protein ligase RNF38

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 RNF38 between cysteines 463 and 489 (413 and 439 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
4v3k
Structure name
rnf38-ubch5b-ub complex
Structure deposition date
2014-10-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
19
% buried
nan
Peptide accession
Q9H0F5
Residue number A
463
Residue number B
489
Peptide name
E3 ubiquitin-protein ligase RNF38

Ligandability

Cysteine 463 of E3 ubiquitin-protein ligase RNF38

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 489 of E3 ubiquitin-protein ligase RNF38

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 RNF38 between cysteines 463 and 468 (413 and 418 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
4v3k
Structure name
rnf38-ubch5b-ub complex
Structure deposition date
2014-10-20
Thiol separation (Å)
8
Half-sphere exposure sum ?
58
Minimum pKa ?
9
% buried
nan
Peptide accession
Q9H0F5
Residue number A
463
Residue number B
468
Peptide name
E3 ubiquitin-protein ligase RNF38

Ligandability

Cysteine 463 of E3 ubiquitin-protein ligase RNF38

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 468 of E3 ubiquitin-protein ligase RNF38

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 RNF38 between cysteines 500 and 503 (450 and 453 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
4v3l
Structure name
rnf38-ub-ubch5b-ub complex
Structure deposition date
2014-10-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
81
Minimum pKa ?
18
% buried
nan
Peptide accession
Q9H0F5
Residue number A
500
Residue number B
503
Peptide name
E3 ubiquitin-protein ligase RNF38

Ligandability

Cysteine 500 of E3 ubiquitin-protein ligase RNF38

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 503 of E3 ubiquitin-protein ligase RNF38

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 RNF38 between cysteines 468 and 489 (418 and 439 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
7ojx
Structure name
e2 ube2k covalently linked to donor ub, acceptor di-ub, and ring e3 primed for k48-linked ub chain synthesis
Structure deposition date
2021-05-17
Thiol separation (Å)
8
Half-sphere exposure sum ?
63
Minimum pKa ?
9
% buried
54
Peptide accession
Q9H0F5
Residue number A
468
Residue number B
489
Peptide name
E3 ubiquitin-protein ligase RNF38

Ligandability

Cysteine 468 of E3 ubiquitin-protein ligase RNF38

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 489 of E3 ubiquitin-protein ligase RNF38

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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