E3 ubiquitin-protein ligase LNX
Intramolecular
Cysteine 111 and cysteine 128
Cysteine 14 and cysteine 17
Cysteine 41 and cysteine 61
Cysteine 105 and cysteine 128
Cysteine 105 and cysteine 111
Cysteine 61 and cysteine 64
Cysteine 44 and cysteine 64
Cysteine 44 and cysteine 61
Cysteine 56 and cysteine 75
Cysteine 41 and cysteine 44
More...Cysteine 75 and cysteine 87
Cysteine 56 and cysteine 87
Cysteine 41 and cysteine 64
5h7r D 101 D 118
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase LNX between cysteines 111 and 128 (101 and 118 respectively in this structure).
Details
Redox score ?
86
PDB code
5h7r
Structure name
structural basis of the flanking zinc-finger motifs crucial for the e3 ligase activity of the lnx1 ring domain
Structure deposition date
2016-11-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
7
% buried
12
Peptide accession
Q8TBB1
Residue number A
111
Residue number B
128
Peptide name
E3 ubiquitin-protein ligase LNX
Ligandability
Cysteine 111 of E3 ubiquitin-protein ligase LNX
Cysteine 128 of E3 ubiquitin-protein ligase LNX
5h7s D 4 D 7
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase LNX between cysteines 14 and 17 (4 and 7 respectively in this structure).
Details
Redox score ?
84
PDB code
5h7s
Structure name
structural basis of the flanking zinc-finger motifs crucial for the e3 ligase activity of the lnx1 ring domain
Structure deposition date
2016-11-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
6
% buried
26
Peptide accession
Q8TBB1
Residue number A
14
Residue number B
17
Peptide name
E3 ubiquitin-protein ligase LNX
Ligandability
Cysteine 14 of E3 ubiquitin-protein ligase LNX
Cysteine 17 of E3 ubiquitin-protein ligase LNX
5h7s B 31 B 51
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase LNX between cysteines 41 and 61 (31 and 51 respectively in this structure).
Details
Redox score ?
81
PDB code
5h7s
Structure name
structural basis of the flanking zinc-finger motifs crucial for the e3 ligase activity of the lnx1 ring domain
Structure deposition date
2016-11-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
6
% buried
nan
Peptide accession
Q8TBB1
Residue number A
41
Residue number B
61
Peptide name
E3 ubiquitin-protein ligase LNX
Ligandability
Cysteine 41 of E3 ubiquitin-protein ligase LNX
Cysteine 61 of E3 ubiquitin-protein ligase LNX
5h7r D 95 D 118
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase LNX between cysteines 105 and 128 (95 and 118 respectively in this structure).
Details
Redox score ?
80
PDB code
5h7r
Structure name
structural basis of the flanking zinc-finger motifs crucial for the e3 ligase activity of the lnx1 ring domain
Structure deposition date
2016-11-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
9
% buried
24
Peptide accession
Q8TBB1
Residue number A
105
Residue number B
128
Peptide name
E3 ubiquitin-protein ligase LNX
Ligandability
Cysteine 105 of E3 ubiquitin-protein ligase LNX
Cysteine 128 of E3 ubiquitin-protein ligase LNX
5h7s D 95 D 101
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase LNX between cysteines 105 and 111 (95 and 101 respectively in this structure).
Details
Redox score ?
80
PDB code
5h7s
Structure name
structural basis of the flanking zinc-finger motifs crucial for the e3 ligase activity of the lnx1 ring domain
Structure deposition date
2016-11-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
9
% buried
28
Peptide accession
Q8TBB1
Residue number A
105
Residue number B
111
Peptide name
E3 ubiquitin-protein ligase LNX
Ligandability
Cysteine 105 of E3 ubiquitin-protein ligase LNX
Cysteine 111 of E3 ubiquitin-protein ligase LNX
5h7s D 51 D 54
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase LNX between cysteines 61 and 64 (51 and 54 respectively in this structure).
Details
Redox score ?
78
PDB code
5h7s
Structure name
structural basis of the flanking zinc-finger motifs crucial for the e3 ligase activity of the lnx1 ring domain
Structure deposition date
2016-11-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
6
% buried
94
Peptide accession
Q8TBB1
Residue number A
61
Residue number B
64
Peptide name
E3 ubiquitin-protein ligase LNX
Ligandability
Cysteine 61 of E3 ubiquitin-protein ligase LNX
Cysteine 64 of E3 ubiquitin-protein ligase LNX
5h7r D 34 D 54
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase LNX between cysteines 44 and 64 (34 and 54 respectively in this structure).
Details
Redox score ?
76
PDB code
5h7r
Structure name
structural basis of the flanking zinc-finger motifs crucial for the e3 ligase activity of the lnx1 ring domain
Structure deposition date
2016-11-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
9
% buried
42
Peptide accession
Q8TBB1
Residue number A
44
Residue number B
64
Peptide name
E3 ubiquitin-protein ligase LNX
Ligandability
Cysteine 44 of E3 ubiquitin-protein ligase LNX
Cysteine 64 of E3 ubiquitin-protein ligase LNX
5h7s D 34 D 51
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase LNX between cysteines 44 and 61 (34 and 51 respectively in this structure).
Details
Redox score ?
76
PDB code
5h7s
Structure name
structural basis of the flanking zinc-finger motifs crucial for the e3 ligase activity of the lnx1 ring domain
Structure deposition date
2016-11-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
72
Minimum pKa ?
6
% buried
96
Peptide accession
Q8TBB1
Residue number A
44
Residue number B
61
Peptide name
E3 ubiquitin-protein ligase LNX
Ligandability
Cysteine 44 of E3 ubiquitin-protein ligase LNX
Cysteine 61 of E3 ubiquitin-protein ligase LNX
5h7s B 46 B 65
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase LNX between cysteines 56 and 75 (46 and 65 respectively in this structure).
Details
Redox score ?
74
PDB code
5h7s
Structure name
structural basis of the flanking zinc-finger motifs crucial for the e3 ligase activity of the lnx1 ring domain
Structure deposition date
2016-11-21
Thiol separation (Å)
3
Half-sphere exposure sum ?
62
Minimum pKa ?
10
% buried
nan
Peptide accession
Q8TBB1
Residue number A
56
Residue number B
75
Peptide name
E3 ubiquitin-protein ligase LNX
Ligandability
Cysteine 56 of E3 ubiquitin-protein ligase LNX
Cysteine 75 of E3 ubiquitin-protein ligase LNX
5h7s D 31 D 34
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase LNX between cysteines 41 and 44 (31 and 34 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
5h7s
Structure name
structural basis of the flanking zinc-finger motifs crucial for the e3 ligase activity of the lnx1 ring domain
Structure deposition date
2016-11-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
71
Minimum pKa ?
15
% buried
nan
Peptide accession
Q8TBB1
Residue number A
41
Residue number B
44
Peptide name
E3 ubiquitin-protein ligase LNX
Ligandability
Cysteine 41 of E3 ubiquitin-protein ligase LNX
Cysteine 44 of E3 ubiquitin-protein ligase LNX
5h7s D 65 D 77
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase LNX between cysteines 75 and 87 (65 and 77 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
5h7s
Structure name
structural basis of the flanking zinc-finger motifs crucial for the e3 ligase activity of the lnx1 ring domain
Structure deposition date
2016-11-21
Thiol separation (Å)
8
Half-sphere exposure sum ?
60
Minimum pKa ?
11
% buried
nan
Peptide accession
Q8TBB1
Residue number A
75
Residue number B
87
Peptide name
E3 ubiquitin-protein ligase LNX
Ligandability
Cysteine 75 of E3 ubiquitin-protein ligase LNX
Cysteine 87 of E3 ubiquitin-protein ligase LNX
5h7s B 46 B 77
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase LNX between cysteines 56 and 87 (46 and 77 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
5h7s
Structure name
structural basis of the flanking zinc-finger motifs crucial for the e3 ligase activity of the lnx1 ring domain
Structure deposition date
2016-11-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
55
Minimum pKa ?
10
% buried
49
Peptide accession
Q8TBB1
Residue number A
56
Residue number B
87
Peptide name
E3 ubiquitin-protein ligase LNX
Ligandability
Cysteine 56 of E3 ubiquitin-protein ligase LNX
Cysteine 87 of E3 ubiquitin-protein ligase LNX
5h7s D 31 D 54
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase LNX between cysteines 41 and 64 (31 and 54 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
5h7s
Structure name
structural basis of the flanking zinc-finger motifs crucial for the e3 ligase activity of the lnx1 ring domain
Structure deposition date
2016-11-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
24
% buried
nan
Peptide accession
Q8TBB1
Residue number A
41
Residue number B
64
Peptide name
E3 ubiquitin-protein ligase LNX
Ligandability
Cysteine 41 of E3 ubiquitin-protein ligase LNX
Cysteine 64 of E3 ubiquitin-protein ligase LNX
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