E3 ubiquitin-protein ligase RNF125
Intramolecular
Cysteine 100 and cysteine 103
Cysteine 103 and cysteine 119
Cysteine 52 and cysteine 75
Cysteine 52 and cysteine 72
Cysteine 37 and cysteine 57
Cysteine 100 and cysteine 119
Cysteine 40 and cysteine 57
Cysteine 72 and cysteine 75
Cysteine 37 and cysteine 40
Cysteine 40 and cysteine 60
More...Cysteine 37 and cysteine 60
Cysteine 57 and cysteine 60
5dka B 100 B 103
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF125 between cysteines 100 and 103.
Details
Redox score ?
90
PDB code
5dka
Structure name
a c2hc zinc finger is essential for the activity of the ring ubiquitin ligase rnf125
Structure deposition date
2015-09-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
45
Minimum pKa ?
5
% buried
5
Peptide accession
Q96EQ8
Residue number A
100
Residue number B
103
Peptide name
E3 ubiquitin-protein ligase RNF125
Ligandability
Cysteine 100 of E3 ubiquitin-protein ligase RNF125
Cysteine 103 of E3 ubiquitin-protein ligase RNF125
5dka B 103 B 119
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF125 between cysteines 103 and 119.
Details
Redox score ?
88
PDB code
5dka
Structure name
a c2hc zinc finger is essential for the activity of the ring ubiquitin ligase rnf125
Structure deposition date
2015-09-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
45
Minimum pKa ?
5
% buried
2
Peptide accession
Q96EQ8
Residue number A
103
Residue number B
119
Peptide name
E3 ubiquitin-protein ligase RNF125
Ligandability
Cysteine 103 of E3 ubiquitin-protein ligase RNF125
Cysteine 119 of E3 ubiquitin-protein ligase RNF125
5dka A 52 A 75
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF125 between cysteines 52 and 75.
Details
Redox score ?
87
PDB code
5dka
Structure name
a c2hc zinc finger is essential for the activity of the ring ubiquitin ligase rnf125
Structure deposition date
2015-09-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
40
Minimum pKa ?
5
% buried
4
Peptide accession
Q96EQ8
Residue number A
52
Residue number B
75
Peptide name
E3 ubiquitin-protein ligase RNF125
Ligandability
Cysteine 52 of E3 ubiquitin-protein ligase RNF125
Cysteine 75 of E3 ubiquitin-protein ligase RNF125
5dka B 52 B 72
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF125 between cysteines 52 and 72.
Details
Redox score ?
86
PDB code
5dka
Structure name
a c2hc zinc finger is essential for the activity of the ring ubiquitin ligase rnf125
Structure deposition date
2015-09-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
5
% buried
18
Peptide accession
Q96EQ8
Residue number A
52
Residue number B
72
Peptide name
E3 ubiquitin-protein ligase RNF125
Ligandability
Cysteine 52 of E3 ubiquitin-protein ligase RNF125
Cysteine 72 of E3 ubiquitin-protein ligase RNF125
5dka A 37 A 57
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF125 between cysteines 37 and 57.
Details
Redox score ?
84
PDB code
5dka
Structure name
a c2hc zinc finger is essential for the activity of the ring ubiquitin ligase rnf125
Structure deposition date
2015-09-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
4
% buried
nan
Peptide accession
Q96EQ8
Residue number A
37
Residue number B
57
Peptide name
E3 ubiquitin-protein ligase RNF125
Ligandability
Cysteine 37 of E3 ubiquitin-protein ligase RNF125
Cysteine 57 of E3 ubiquitin-protein ligase RNF125
5dka A 100 A 119
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF125 between cysteines 100 and 119.
Details
Redox score ?
82
PDB code
5dka
Structure name
a c2hc zinc finger is essential for the activity of the ring ubiquitin ligase rnf125
Structure deposition date
2015-09-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
8
% buried
8
Peptide accession
Q96EQ8
Residue number A
100
Residue number B
119
Peptide name
E3 ubiquitin-protein ligase RNF125
Ligandability
Cysteine 100 of E3 ubiquitin-protein ligase RNF125
Cysteine 119 of E3 ubiquitin-protein ligase RNF125
5dka A 40 A 57
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF125 between cysteines 40 and 57.
Details
Redox score ?
81
PDB code
5dka
Structure name
a c2hc zinc finger is essential for the activity of the ring ubiquitin ligase rnf125
Structure deposition date
2015-09-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
4
% buried
55
Peptide accession
Q96EQ8
Residue number A
40
Residue number B
57
Peptide name
E3 ubiquitin-protein ligase RNF125
Ligandability
Cysteine 40 of E3 ubiquitin-protein ligase RNF125
Cysteine 57 of E3 ubiquitin-protein ligase RNF125
5dka A 72 A 75
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF125 between cysteines 72 and 75.
Details
Redox score ?
79
PDB code
5dka
Structure name
a c2hc zinc finger is essential for the activity of the ring ubiquitin ligase rnf125
Structure deposition date
2015-09-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
8
% buried
12
Peptide accession
Q96EQ8
Residue number A
72
Residue number B
75
Peptide name
E3 ubiquitin-protein ligase RNF125
Ligandability
Cysteine 72 of E3 ubiquitin-protein ligase RNF125
Cysteine 75 of E3 ubiquitin-protein ligase RNF125
5dka A 37 A 40
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF125 between cysteines 37 and 40.
Details
Redox score ?
68
PDB code
5dka
Structure name
a c2hc zinc finger is essential for the activity of the ring ubiquitin ligase rnf125
Structure deposition date
2015-09-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
13
% buried
nan
Peptide accession
Q96EQ8
Residue number A
37
Residue number B
40
Peptide name
E3 ubiquitin-protein ligase RNF125
Ligandability
Cysteine 37 of E3 ubiquitin-protein ligase RNF125
Cysteine 40 of E3 ubiquitin-protein ligase RNF125
5dka B 40 B 60
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF125 between cysteines 40 and 60.
Details
Redox score ?
63
PDB code
5dka
Structure name
a c2hc zinc finger is essential for the activity of the ring ubiquitin ligase rnf125
Structure deposition date
2015-09-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
13
% buried
56
Peptide accession
Q96EQ8
Residue number A
40
Residue number B
60
Peptide name
E3 ubiquitin-protein ligase RNF125
Ligandability
Cysteine 40 of E3 ubiquitin-protein ligase RNF125
Cysteine 60 of E3 ubiquitin-protein ligase RNF125
5dka A 37 A 60
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF125 between cysteines 37 and 60. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
5dka
Structure name
a c2hc zinc finger is essential for the activity of the ring ubiquitin ligase rnf125
Structure deposition date
2015-09-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
22
% buried
nan
Peptide accession
Q96EQ8
Residue number A
37
Residue number B
60
Peptide name
E3 ubiquitin-protein ligase RNF125
Ligandability
Cysteine 37 of E3 ubiquitin-protein ligase RNF125
Cysteine 60 of E3 ubiquitin-protein ligase RNF125
5dka B 57 B 60
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF125 between cysteines 57 and 60. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
5dka
Structure name
a c2hc zinc finger is essential for the activity of the ring ubiquitin ligase rnf125
Structure deposition date
2015-09-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
22
% buried
nan
Peptide accession
Q96EQ8
Residue number A
57
Residue number B
60
Peptide name
E3 ubiquitin-protein ligase RNF125
Ligandability
Cysteine 57 of E3 ubiquitin-protein ligase RNF125
Cysteine 60 of E3 ubiquitin-protein ligase RNF125
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