ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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E3 ubiquitin-protein ligase FANCL

Intramolecular
Cysteine 324 and cysteine 362
Cysteine 329 and cysteine 362
Cysteine 359 and cysteine 362
Cysteine 324 and cysteine 329
Cysteine 329 and cysteine 359
Cysteine 307 and cysteine 310
Cysteine 324 and cysteine 359
Cysteine 310 and cysteine 337
Cysteine 307 and cysteine 337
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase FANCL between cysteines 324 and 362.

Details

Redox score ?
88
PDB code
4ccg
Structure name
structure of an e2-e3 complex
Structure deposition date
2013-10-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
5
% buried
6
Peptide accession
Q9NW38
Residue number A
324
Residue number B
362
Peptide name
E3 ubiquitin-protein ligase FANCL

Ligandability

Cysteine 324 of E3 ubiquitin-protein ligase FANCL

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 362 of E3 ubiquitin-protein ligase FANCL

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 FANCL between cysteines 329 and 362.

Details

Redox score ?
88
PDB code
4ccg
Structure name
structure of an e2-e3 complex
Structure deposition date
2013-10-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
42
Minimum pKa ?
5
% buried
6
Peptide accession
Q9NW38
Residue number A
329
Residue number B
362
Peptide name
E3 ubiquitin-protein ligase FANCL

Ligandability

Cysteine 329 of E3 ubiquitin-protein ligase FANCL

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 362 of E3 ubiquitin-protein ligase FANCL

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 FANCL between cysteines 359 and 362.

Details

Redox score ?
84
PDB code
4ccg
Structure name
structure of an e2-e3 complex
Structure deposition date
2013-10-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
5
% buried
24
Peptide accession
Q9NW38
Residue number A
359
Residue number B
362
Peptide name
E3 ubiquitin-protein ligase FANCL

Ligandability

Cysteine 359 of E3 ubiquitin-protein ligase FANCL

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 362 of E3 ubiquitin-protein ligase FANCL

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 FANCL between cysteines 324 and 329.

Details

Redox score ?
83
PDB code
4ccg
Structure name
structure of an e2-e3 complex
Structure deposition date
2013-10-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
8
% buried
44
Peptide accession
Q9NW38
Residue number A
324
Residue number B
329
Peptide name
E3 ubiquitin-protein ligase FANCL

Ligandability

Cysteine 324 of E3 ubiquitin-protein ligase FANCL

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 329 of E3 ubiquitin-protein ligase FANCL

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 FANCL between cysteines 329 and 359.

Details

Redox score ?
80
PDB code
4ccg
Structure name
structure of an e2-e3 complex
Structure deposition date
2013-10-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
8
% buried
30
Peptide accession
Q9NW38
Residue number A
329
Residue number B
359
Peptide name
E3 ubiquitin-protein ligase FANCL

Ligandability

Cysteine 329 of E3 ubiquitin-protein ligase FANCL

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 359 of E3 ubiquitin-protein ligase FANCL

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 FANCL between cysteines 307 and 310.

Details

Redox score ?
76
PDB code
4ccg
Structure name
structure of an e2-e3 complex
Structure deposition date
2013-10-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
74
Minimum pKa ?
7
% buried
nan
Peptide accession
Q9NW38
Residue number A
307
Residue number B
310
Peptide name
E3 ubiquitin-protein ligase FANCL

Ligandability

Cysteine 307 of E3 ubiquitin-protein ligase FANCL

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 310 of E3 ubiquitin-protein ligase FANCL

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 FANCL between cysteines 324 and 359.

Details

Redox score ?
74
PDB code
4ccg
Structure name
structure of an e2-e3 complex
Structure deposition date
2013-10-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
10
% buried
52
Peptide accession
Q9NW38
Residue number A
324
Residue number B
359
Peptide name
E3 ubiquitin-protein ligase FANCL

Ligandability

Cysteine 324 of E3 ubiquitin-protein ligase FANCL

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 359 of E3 ubiquitin-protein ligase FANCL

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 FANCL between cysteines 310 and 337.

Details

Redox score ?
71
PDB code
4ccg
Structure name
structure of an e2-e3 complex
Structure deposition date
2013-10-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
88
Minimum pKa ?
8
% buried
80
Peptide accession
Q9NW38
Residue number A
310
Residue number B
337
Peptide name
E3 ubiquitin-protein ligase FANCL

Ligandability

Cysteine 310 of E3 ubiquitin-protein ligase FANCL

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 337 of E3 ubiquitin-protein ligase FANCL

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 FANCL between cysteines 307 and 337. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
4ccg
Structure name
structure of an e2-e3 complex
Structure deposition date
2013-10-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
82
Minimum pKa ?
20
% buried
nan
Peptide accession
Q9NW38
Residue number A
307
Residue number B
337
Peptide name
E3 ubiquitin-protein ligase FANCL

Ligandability

Cysteine 307 of E3 ubiquitin-protein ligase FANCL

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 337 of E3 ubiquitin-protein ligase FANCL

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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