ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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E3 ubiquitin-protein ligase RNF8

Intermolecular
Cysteine 456 and cysteine 456
Intramolecular
Cysteine 418 and cysteine 437 L
Cysteine 403 and cysteine 406
Cysteine 418 and cysteine 440 L
Cysteine 403 and cysteine 423
Cysteine 406 and cysteine 423
Cysteine 423 and cysteine 426
Cysteine 403 and cysteine 426
Cysteine 406 and cysteine 426
Cysteine 437 and cysteine 440 L
Cysteine 19 and cysteine 135
A redox-regulated disulphide may form between two units of E3 ubiquitin-protein ligase RNF8 at cysteines 456 and 456. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
4orh
Structure name
crystal structure of rnf8 bound to the ubc13/mms2 heterodimer
Structure deposition date
2014-02-11
Thiol separation (Å)
7
Half-sphere exposure sum ?
75
Minimum pKa ?
12
% buried
96
Peptide A name
E3 ubiquitin-protein ligase RNF8
Peptide B name
E3 ubiquitin-protein ligase RNF8
Peptide A accession
O76064
Peptide B accession
O76064
Peptide A residue number
456
Peptide B residue number
456

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 RNF8 between cysteines 418 and 437.

Details

Redox score ?
87
PDB code
4orh
Structure name
crystal structure of rnf8 bound to the ubc13/mms2 heterodimer
Structure deposition date
2014-02-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
67
Minimum pKa ?
1
% buried
76
Peptide accession
O76064
Residue number A
418
Residue number B
437
Peptide name
E3 ubiquitin-protein ligase RNF8

Ligandability

Cysteine 418 of E3 ubiquitin-protein ligase RNF8

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 437 of E3 ubiquitin-protein ligase RNF8

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF8 between cysteines 403 and 406.

Details

Redox score ?
85
PDB code
4orh
Structure name
crystal structure of rnf8 bound to the ubc13/mms2 heterodimer
Structure deposition date
2014-02-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
5
% buried
nan
Peptide accession
O76064
Residue number A
403
Residue number B
406
Peptide name
E3 ubiquitin-protein ligase RNF8

Ligandability

Cysteine 403 of E3 ubiquitin-protein ligase RNF8

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 406 of E3 ubiquitin-protein ligase RNF8

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 RNF8 between cysteines 418 and 440.

Details

Redox score ?
82
PDB code
4ayc
Structure name
rnf8 ring domain structure
Structure deposition date
2012-06-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
43
Minimum pKa ?
7
% buried
22
Peptide accession
O76064
Residue number A
418
Residue number B
440
Peptide name
E3 ubiquitin-protein ligase RNF8

Ligandability

Cysteine 418 of E3 ubiquitin-protein ligase RNF8

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 440 of E3 ubiquitin-protein ligase RNF8

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF8 between cysteines 403 and 423.

Details

Redox score ?
81
PDB code
4whv
Structure name
e3 ubiquitin-protein ligase rnf8 in complex with ubiquitin-conjugating enzyme e2 n and polyubiquitin-b
Structure deposition date
2014-09-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
71
Minimum pKa ?
5
% buried
nan
Peptide accession
O76064
Residue number A
403
Residue number B
423
Peptide name
E3 ubiquitin-protein ligase RNF8

Ligandability

Cysteine 403 of E3 ubiquitin-protein ligase RNF8

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 423 of E3 ubiquitin-protein ligase RNF8

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 RNF8 between cysteines 406 and 423.

Details

Redox score ?
66
PDB code
4orh
Structure name
crystal structure of rnf8 bound to the ubc13/mms2 heterodimer
Structure deposition date
2014-02-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
13
% buried
nan
Peptide accession
O76064
Residue number A
406
Residue number B
423
Peptide name
E3 ubiquitin-protein ligase RNF8

Ligandability

Cysteine 406 of E3 ubiquitin-protein ligase RNF8

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 423 of E3 ubiquitin-protein ligase RNF8

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 RNF8 between cysteines 423 and 426.

Details

Redox score ?
62
PDB code
4orh
Structure name
crystal structure of rnf8 bound to the ubc13/mms2 heterodimer
Structure deposition date
2014-02-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
67
Minimum pKa ?
13
% buried
62
Peptide accession
O76064
Residue number A
423
Residue number B
426
Peptide name
E3 ubiquitin-protein ligase RNF8

Ligandability

Cysteine 423 of E3 ubiquitin-protein ligase RNF8

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 426 of E3 ubiquitin-protein ligase RNF8

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 RNF8 between cysteines 403 and 426. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
59
PDB code
4orh
Structure name
crystal structure of rnf8 bound to the ubc13/mms2 heterodimer
Structure deposition date
2014-02-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
14
% buried
98
Peptide accession
O76064
Residue number A
403
Residue number B
426
Peptide name
E3 ubiquitin-protein ligase RNF8

Ligandability

Cysteine 403 of E3 ubiquitin-protein ligase RNF8

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 426 of E3 ubiquitin-protein ligase RNF8

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 RNF8 between cysteines 406 and 426. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
59
PDB code
4whv
Structure name
e3 ubiquitin-protein ligase rnf8 in complex with ubiquitin-conjugating enzyme e2 n and polyubiquitin-b
Structure deposition date
2014-09-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
75
Minimum pKa ?
14
% buried
86
Peptide accession
O76064
Residue number A
406
Residue number B
426
Peptide name
E3 ubiquitin-protein ligase RNF8

Ligandability

Cysteine 406 of E3 ubiquitin-protein ligase RNF8

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 426 of E3 ubiquitin-protein ligase RNF8

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 RNF8 between cysteines 437 and 440. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
4whv
Structure name
e3 ubiquitin-protein ligase rnf8 in complex with ubiquitin-conjugating enzyme e2 n and polyubiquitin-b
Structure deposition date
2014-09-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
79
Minimum pKa ?
18
% buried
nan
Peptide accession
O76064
Residue number A
437
Residue number B
440
Peptide name
E3 ubiquitin-protein ligase RNF8

Ligandability

Cysteine 437 of E3 ubiquitin-protein ligase RNF8

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 440 of E3 ubiquitin-protein ligase RNF8

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF8 between cysteines 19 and 135. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
2pie
Structure name
crystal structure of the fha domain of rnf8 in complex with its optimal phosphopeptide
Structure deposition date
2007-04-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
10
% buried
36
Peptide accession
O76064
Residue number A
19
Residue number B
135
Peptide name
E3 ubiquitin-protein ligase RNF8

Ligandability

Cysteine 19 of E3 ubiquitin-protein ligase RNF8

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 135 of E3 ubiquitin-protein ligase RNF8

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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