E3 ubiquitin-protein ligase RNF168
Intramolecular
Cysteine 31 and cysteine 54
Cysteine 51 and cysteine 54
Cysteine 16 and cysteine 19
Cysteine 31 and cysteine 51
Cysteine 36 and cysteine 39
Cysteine 16 and cysteine 36
Cysteine 19 and cysteine 36
Cysteine 19 and cysteine 39
Cysteine 16 and cysteine 39
Cysteine 50 and cysteine 54
More...Cysteine 14 and cysteine 88
Cysteine 50 and cysteine 51
Cysteine 31 and cysteine 50
3l11 A 31 A 54
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF168 between cysteines 31 and 54.
Details
Redox score ?
87
PDB code
3l11
Structure name
crystal structure of the ring domain of rnf168
Structure deposition date
2009-12-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
34
Minimum pKa ?
6
% buried
8
Peptide accession
Q8IYW5
Residue number A
31
Residue number B
54
Peptide name
E3 ubiquitin-protein ligase RNF168
Ligandability
Cysteine 31 of E3 ubiquitin-protein ligase RNF168
Cysteine 54 of E3 ubiquitin-protein ligase RNF168
4gb0 A 51 A 54
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF168 between cysteines 51 and 54.
Details
Redox score ?
82
PDB code
4gb0
Structure name
crystal structure of the ring domain of rnf168
Structure deposition date
2012-07-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
7
% buried
8
Peptide accession
Q8IYW5
Residue number A
51
Residue number B
54
Peptide name
E3 ubiquitin-protein ligase RNF168
Ligandability
Cysteine 51 of E3 ubiquitin-protein ligase RNF168
Cysteine 54 of E3 ubiquitin-protein ligase RNF168
3l11 A 16 A 19
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF168 between cysteines 16 and 19.
Details
Redox score ?
79
PDB code
3l11
Structure name
crystal structure of the ring domain of rnf168
Structure deposition date
2009-12-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
8
% buried
40
Peptide accession
Q8IYW5
Residue number A
16
Residue number B
19
Peptide name
E3 ubiquitin-protein ligase RNF168
Ligandability
Cysteine 16 of E3 ubiquitin-protein ligase RNF168
Cysteine 19 of E3 ubiquitin-protein ligase RNF168
3l11 A 31 A 51
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF168 between cysteines 31 and 51.
Details
Redox score ?
79
PDB code
3l11
Structure name
crystal structure of the ring domain of rnf168
Structure deposition date
2009-12-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
9
% buried
23
Peptide accession
Q8IYW5
Residue number A
31
Residue number B
51
Peptide name
E3 ubiquitin-protein ligase RNF168
Ligandability
Cysteine 31 of E3 ubiquitin-protein ligase RNF168
Cysteine 51 of E3 ubiquitin-protein ligase RNF168
3l11 A 36 A 39
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF168 between cysteines 36 and 39.
Details
Redox score ?
79
PDB code
3l11
Structure name
crystal structure of the ring domain of rnf168
Structure deposition date
2009-12-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
7
% buried
45
Peptide accession
Q8IYW5
Residue number A
36
Residue number B
39
Peptide name
E3 ubiquitin-protein ligase RNF168
Ligandability
Cysteine 36 of E3 ubiquitin-protein ligase RNF168
Cysteine 39 of E3 ubiquitin-protein ligase RNF168
4gb0 A 16 A 36
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF168 between cysteines 16 and 36.
Details
Redox score ?
79
PDB code
4gb0
Structure name
crystal structure of the ring domain of rnf168
Structure deposition date
2012-07-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
6
% buried
38
Peptide accession
Q8IYW5
Residue number A
16
Residue number B
36
Peptide name
E3 ubiquitin-protein ligase RNF168
Ligandability
Cysteine 16 of E3 ubiquitin-protein ligase RNF168
Cysteine 36 of E3 ubiquitin-protein ligase RNF168
3l11 A 19 A 36
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF168 between cysteines 19 and 36.
Details
Redox score ?
79
PDB code
3l11
Structure name
crystal structure of the ring domain of rnf168
Structure deposition date
2009-12-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
7
% buried
40
Peptide accession
Q8IYW5
Residue number A
19
Residue number B
36
Peptide name
E3 ubiquitin-protein ligase RNF168
Ligandability
Cysteine 19 of E3 ubiquitin-protein ligase RNF168
Cysteine 36 of E3 ubiquitin-protein ligase RNF168
3l11 A 19 A 39
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF168 between cysteines 19 and 39.
Details
Redox score ?
77
PDB code
3l11
Structure name
crystal structure of the ring domain of rnf168
Structure deposition date
2009-12-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
8
% buried
35
Peptide accession
Q8IYW5
Residue number A
19
Residue number B
39
Peptide name
E3 ubiquitin-protein ligase RNF168
Ligandability
Cysteine 19 of E3 ubiquitin-protein ligase RNF168
Cysteine 39 of E3 ubiquitin-protein ligase RNF168
3l11 A 16 A 39
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF168 between cysteines 16 and 39.
Details
Redox score ?
72
PDB code
3l11
Structure name
crystal structure of the ring domain of rnf168
Structure deposition date
2009-12-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
11
% buried
45
Peptide accession
Q8IYW5
Residue number A
16
Residue number B
39
Peptide name
E3 ubiquitin-protein ligase RNF168
Ligandability
Cysteine 16 of E3 ubiquitin-protein ligase RNF168
Cysteine 39 of E3 ubiquitin-protein ligase RNF168
3l11 A 50 A 54
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF168 between cysteines 50 and 54. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
52
PDB code
3l11
Structure name
crystal structure of the ring domain of rnf168
Structure deposition date
2009-12-10
Thiol separation (Å)
9
Half-sphere exposure sum ?
44
Minimum pKa ?
6
% buried
0
Peptide accession
Q8IYW5
Residue number A
50
Residue number B
54
Peptide name
E3 ubiquitin-protein ligase RNF168
Ligandability
Cysteine 50 of E3 ubiquitin-protein ligase RNF168
Cysteine 54 of E3 ubiquitin-protein ligase RNF168
4gb0 A 14 A 88
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF168 between cysteines 14 and 88. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
4gb0
Structure name
crystal structure of the ring domain of rnf168
Structure deposition date
2012-07-26
Thiol separation (Å)
8
Half-sphere exposure sum ?
59
Minimum pKa ?
10
% buried
26
Peptide accession
Q8IYW5
Residue number A
14
Residue number B
88
Peptide name
E3 ubiquitin-protein ligase RNF168
Ligandability
Cysteine 14 of E3 ubiquitin-protein ligase RNF168
Cysteine 88 of E3 ubiquitin-protein ligase RNF168
3l11 A 50 A 51
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF168 between cysteines 50 and 51. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
3l11
Structure name
crystal structure of the ring domain of rnf168
Structure deposition date
2009-12-10
Thiol separation (Å)
9
Half-sphere exposure sum ?
62
Minimum pKa ?
8
% buried
16
Peptide accession
Q8IYW5
Residue number A
50
Residue number B
51
Peptide name
E3 ubiquitin-protein ligase RNF168
Ligandability
Cysteine 50 of E3 ubiquitin-protein ligase RNF168
Cysteine 51 of E3 ubiquitin-protein ligase RNF168
4gb0 A 31 A 50
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF168 between cysteines 31 and 50. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
4gb0
Structure name
crystal structure of the ring domain of rnf168
Structure deposition date
2012-07-26
Thiol separation (Å)
10
Half-sphere exposure sum ?
44
Minimum pKa ?
9
% buried
5
Peptide accession
Q8IYW5
Residue number A
31
Residue number B
50
Peptide name
E3 ubiquitin-protein ligase RNF168
Ligandability
Cysteine 31 of E3 ubiquitin-protein ligase RNF168
Cysteine 50 of E3 ubiquitin-protein ligase RNF168
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