E3 ubiquitin-protein ligase RNF146
Intramolecular
Cysteine 37 and cysteine 57
Cysteine 37 and cysteine 40
Cysteine 37 and cysteine 44
Cysteine 41 and cysteine 58
Cysteine 52 and cysteine 74
Cysteine 44 and cysteine 57
Cysteine 72 and cysteine 75
Cysteine 53 and cysteine 72
Cysteine 57 and cysteine 60
Cysteine 40 and cysteine 44
More...Cysteine 44 and cysteine 60
Cysteine 41 and cysteine 61
Cysteine 37 and cysteine 71
Cysteine 38 and cysteine 61
2d8t A 18 A 38
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF146 between cysteines 37 and 57 (18 and 38 respectively in this structure).
Details
Redox score ?
92
PDB code
2d8t
Structure name
solution structure of the ring domain of the human ring finger protein 146
Structure deposition date
2005-12-08
Thiol separation (Å)
3
Half-sphere exposure sum ?
55
Minimum pKa ?
5
% buried
7
Peptide accession
Q9NTX7
Residue number A
37
Residue number B
57
Peptide name
E3 ubiquitin-protein ligase RNF146
Ligandability
Cysteine 37 of E3 ubiquitin-protein ligase RNF146
Cysteine 57 of E3 ubiquitin-protein ligase RNF146
2d8t A 18 A 21
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF146 between cysteines 37 and 40 (18 and 21 respectively in this structure).
Details
Redox score ?
91
PDB code
2d8t
Structure name
solution structure of the ring domain of the human ring finger protein 146
Structure deposition date
2005-12-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
5
% buried
6
Peptide accession
Q9NTX7
Residue number A
37
Residue number B
40
Peptide name
E3 ubiquitin-protein ligase RNF146
Ligandability
Cysteine 37 of E3 ubiquitin-protein ligase RNF146
Cysteine 40 of E3 ubiquitin-protein ligase RNF146
2d8t A 18 A 25
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF146 between cysteines 37 and 44 (18 and 25 respectively in this structure).
Details
Redox score ?
89
PDB code
2d8t
Structure name
solution structure of the ring domain of the human ring finger protein 146
Structure deposition date
2005-12-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
5
% buried
6
Peptide accession
Q9NTX7
Residue number A
37
Residue number B
44
Peptide name
E3 ubiquitin-protein ligase RNF146
Ligandability
Cysteine 37 of E3 ubiquitin-protein ligase RNF146
Cysteine 44 of E3 ubiquitin-protein ligase RNF146
4qpl C 39 C 56
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF146 between cysteines 41 and 58 (39 and 56 respectively in this structure).
Details
Redox score ?
85
PDB code
4qpl
Structure name
crystal structure of rnf146(ring-wwe)/ubch5a/iso-adpr complex
Structure deposition date
2014-06-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
81
Minimum pKa ?
1
% buried
84
Peptide accession
Q9CZW6
Residue number A
41
Residue number B
58
Peptide name
E3 ubiquitin-protein ligase RNF146
Ligandability
Cysteine 41 of E3 ubiquitin-protein ligase RNF146
Cysteine 58 of E3 ubiquitin-protein ligase RNF146
2d8t A 33 A 55
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF146 between cysteines 52 and 74 (33 and 55 respectively in this structure).
Details
Redox score ?
84
PDB code
2d8t
Structure name
solution structure of the ring domain of the human ring finger protein 146
Structure deposition date
2005-12-08
Thiol separation (Å)
3
Half-sphere exposure sum ?
35
Minimum pKa ?
8
% buried
0
Peptide accession
Q9NTX7
Residue number A
52
Residue number B
74
Peptide name
E3 ubiquitin-protein ligase RNF146
Ligandability
Cysteine 52 of E3 ubiquitin-protein ligase RNF146
Cysteine 74 of E3 ubiquitin-protein ligase RNF146
2d8t A 25 A 38
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF146 between cysteines 44 and 57 (25 and 38 respectively in this structure).
Details
Redox score ?
83
PDB code
2d8t
Structure name
solution structure of the ring domain of the human ring finger protein 146
Structure deposition date
2005-12-08
Thiol separation (Å)
3
Half-sphere exposure sum ?
53
Minimum pKa ?
10
% buried
2
Peptide accession
Q9NTX7
Residue number A
44
Residue number B
57
Peptide name
E3 ubiquitin-protein ligase RNF146
Ligandability
Cysteine 44 of E3 ubiquitin-protein ligase RNF146
Cysteine 57 of E3 ubiquitin-protein ligase RNF146
4qpl C 70 C 73
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF146 between cysteines 72 and 75 (70 and 73 respectively in this structure).
Details
Redox score ?
78
PDB code
4qpl
Structure name
crystal structure of rnf146(ring-wwe)/ubch5a/iso-adpr complex
Structure deposition date
2014-06-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
7
% buried
22
Peptide accession
Q9CZW6
Residue number A
72
Residue number B
75
Peptide name
E3 ubiquitin-protein ligase RNF146
Ligandability
Cysteine 72 of E3 ubiquitin-protein ligase RNF146
Cysteine 75 of E3 ubiquitin-protein ligase RNF146
4qpl C 51 C 70
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF146 between cysteines 53 and 72 (51 and 70 respectively in this structure).
Details
Redox score ?
78
PDB code
4qpl
Structure name
crystal structure of rnf146(ring-wwe)/ubch5a/iso-adpr complex
Structure deposition date
2014-06-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
9
% buried
28
Peptide accession
Q9CZW6
Residue number A
53
Residue number B
72
Peptide name
E3 ubiquitin-protein ligase RNF146
Ligandability
Cysteine 53 of E3 ubiquitin-protein ligase RNF146
Cysteine 72 of E3 ubiquitin-protein ligase RNF146
2d8t A 38 A 41
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF146 between cysteines 57 and 60 (38 and 41 respectively in this structure).
Details
Redox score ?
73
PDB code
2d8t
Structure name
solution structure of the ring domain of the human ring finger protein 146
Structure deposition date
2005-12-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
11
% buried
5
Peptide accession
Q9NTX7
Residue number A
57
Residue number B
60
Peptide name
E3 ubiquitin-protein ligase RNF146
Ligandability
Cysteine 57 of E3 ubiquitin-protein ligase RNF146
Cysteine 60 of E3 ubiquitin-protein ligase RNF146
2d8t A 21 A 25
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF146 between cysteines 40 and 44 (21 and 25 respectively in this structure).
Details
Redox score ?
67
PDB code
2d8t
Structure name
solution structure of the ring domain of the human ring finger protein 146
Structure deposition date
2005-12-08
Thiol separation (Å)
6
Half-sphere exposure sum ?
45
Minimum pKa ?
9
% buried
0
Peptide accession
Q9NTX7
Residue number A
40
Residue number B
44
Peptide name
E3 ubiquitin-protein ligase RNF146
Ligandability
Cysteine 40 of E3 ubiquitin-protein ligase RNF146
Cysteine 44 of E3 ubiquitin-protein ligase RNF146
2d8t A 25 A 41
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF146 between cysteines 44 and 60 (25 and 41 respectively in this structure).
Details
Redox score ?
62
PDB code
2d8t
Structure name
solution structure of the ring domain of the human ring finger protein 146
Structure deposition date
2005-12-08
Thiol separation (Å)
7
Half-sphere exposure sum ?
55
Minimum pKa ?
10
% buried
4
Peptide accession
Q9NTX7
Residue number A
44
Residue number B
60
Peptide name
E3 ubiquitin-protein ligase RNF146
Ligandability
Cysteine 44 of E3 ubiquitin-protein ligase RNF146
Cysteine 60 of E3 ubiquitin-protein ligase RNF146
4qpl C 39 C 59
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF146 between cysteines 41 and 61 (39 and 59 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
59
PDB code
4qpl
Structure name
crystal structure of rnf146(ring-wwe)/ubch5a/iso-adpr complex
Structure deposition date
2014-06-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
82
Minimum pKa ?
14
% buried
88
Peptide accession
Q9CZW6
Residue number A
41
Residue number B
61
Peptide name
E3 ubiquitin-protein ligase RNF146
Ligandability
Cysteine 41 of E3 ubiquitin-protein ligase RNF146
Cysteine 61 of E3 ubiquitin-protein ligase RNF146
2d8t A 18 A 52
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF146 between cysteines 37 and 71 (18 and 52 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
2d8t
Structure name
solution structure of the ring domain of the human ring finger protein 146
Structure deposition date
2005-12-08
Thiol separation (Å)
9
Half-sphere exposure sum ?
59
Minimum pKa ?
5
% buried
12
Peptide accession
Q9NTX7
Residue number A
37
Residue number B
71
Peptide name
E3 ubiquitin-protein ligase RNF146
Ligandability
Cysteine 37 of E3 ubiquitin-protein ligase RNF146
Cysteine 71 of E3 ubiquitin-protein ligase RNF146
4qpl A 36 A 59
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF146 between cysteines 38 and 61 (36 and 59 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
4qpl
Structure name
crystal structure of rnf146(ring-wwe)/ubch5a/iso-adpr complex
Structure deposition date
2014-06-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
74
Minimum pKa ?
25
% buried
nan
Peptide accession
Q9CZW6
Residue number A
38
Residue number B
61
Peptide name
E3 ubiquitin-protein ligase RNF146
Ligandability
Cysteine 38 of E3 ubiquitin-protein ligase RNF146
Cysteine 61 of E3 ubiquitin-protein ligase RNF146
If this tool was useful for finding a disulphide, please cite: