E3 ubiquitin-protein ligase MSL2
Intermolecular
Cysteine 221 of Male-specific lethal 1 homolog and cysteine 107 L
Intramolecular
Cysteine 44 and cysteine 67
Cysteine 44 and cysteine 70
Cysteine 62 and cysteine 84
Cysteine 44 and cysteine 47
Cysteine 47 and cysteine 70
Cysteine 47 and cysteine 67
Cysteine 67 and cysteine 70
Cysteine 62 and cysteine 81
Cysteine 44 and cysteine 45
More...Cysteine 45 and cysteine 84
Cysteine 81 and cysteine 84
Cysteine 45 and cysteine 67
Cysteine 45 and cysteine 62
Cysteine 45 and cysteine 70
Cysteine 45 and cysteine 81
Cysteine 45 and cysteine 47
4b7y B 221 D 107
A redox-regulated disulphide may form between cysteine 221 of Male-specific lethal 1 homolog and cysteine 107 of E3 ubiquitin-protein ligase MSL2. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
36
PDB code
4b7y
Structure name
crystal structure of the msl1-msl2 complex
Structure deposition date
2012-08-24
Thiol separation (Å)
10
Half-sphere exposure sum ?
55
Minimum pKa ?
10
% buried
46
Peptide A name
Male-specific lethal 1 homolog
Peptide B name
E3 ubiquitin-protein ligase MSL2
Peptide A accession
Q68DK7
Peptide B accession
Q9HCI7
Peptide A residue number
221
Peptide B residue number
107
Ligandability
Cysteine 221 of Male-specific lethal 1 homolog
Cysteine 107 of E3 ubiquitin-protein ligase MSL2
4b86 D 44 D 67
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase MSL2 between cysteines 44 and 67.
Details
Redox score ?
89
PDB code
4b86
Structure name
crystal structure of the msl1-msl2 complex (3
Structure deposition date
2012-08-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
5
% buried
0
Peptide accession
Q9HCI7
Residue number A
44
Residue number B
67
Peptide name
E3 ubiquitin-protein ligase MSL2
Ligandability
Cysteine 44 of E3 ubiquitin-protein ligase MSL2
Cysteine 67 of E3 ubiquitin-protein ligase MSL2
4b86 C 44 C 70
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase MSL2 between cysteines 44 and 70.
Details
Redox score ?
86
PDB code
4b86
Structure name
crystal structure of the msl1-msl2 complex (3
Structure deposition date
2012-08-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
6
% buried
16
Peptide accession
Q9HCI7
Residue number A
44
Residue number B
70
Peptide name
E3 ubiquitin-protein ligase MSL2
Ligandability
Cysteine 44 of E3 ubiquitin-protein ligase MSL2
Cysteine 70 of E3 ubiquitin-protein ligase MSL2
4b7y C 62 C 84
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase MSL2 between cysteines 62 and 84.
Details
Redox score ?
83
PDB code
4b7y
Structure name
crystal structure of the msl1-msl2 complex
Structure deposition date
2012-08-24
Thiol separation (Å)
3
Half-sphere exposure sum ?
52
Minimum pKa ?
8
% buried
29
Peptide accession
Q9HCI7
Residue number A
62
Residue number B
84
Peptide name
E3 ubiquitin-protein ligase MSL2
Ligandability
Cysteine 62 of E3 ubiquitin-protein ligase MSL2
Cysteine 84 of E3 ubiquitin-protein ligase MSL2
4b86 L 44 L 47
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase MSL2 between cysteines 44 and 47.
Details
Redox score ?
82
PDB code
4b86
Structure name
crystal structure of the msl1-msl2 complex (3
Structure deposition date
2012-08-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
6
% buried
17
Peptide accession
Q9HCI7
Residue number A
44
Residue number B
47
Peptide name
E3 ubiquitin-protein ligase MSL2
Ligandability
Cysteine 44 of E3 ubiquitin-protein ligase MSL2
Cysteine 47 of E3 ubiquitin-protein ligase MSL2
4b86 C 47 C 70
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase MSL2 between cysteines 47 and 70.
Details
Redox score ?
82
PDB code
4b86
Structure name
crystal structure of the msl1-msl2 complex (3
Structure deposition date
2012-08-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
8
% buried
0
Peptide accession
Q9HCI7
Residue number A
47
Residue number B
70
Peptide name
E3 ubiquitin-protein ligase MSL2
Ligandability
Cysteine 47 of E3 ubiquitin-protein ligase MSL2
Cysteine 70 of E3 ubiquitin-protein ligase MSL2
4b7y C 47 C 67
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase MSL2 between cysteines 47 and 67.
Details
Redox score ?
77
PDB code
4b7y
Structure name
crystal structure of the msl1-msl2 complex
Structure deposition date
2012-08-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
8
% buried
12
Peptide accession
Q9HCI7
Residue number A
47
Residue number B
67
Peptide name
E3 ubiquitin-protein ligase MSL2
Ligandability
Cysteine 47 of E3 ubiquitin-protein ligase MSL2
Cysteine 67 of E3 ubiquitin-protein ligase MSL2
4b86 G 67 G 70
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase MSL2 between cysteines 67 and 70.
Details
Redox score ?
77
PDB code
4b86
Structure name
crystal structure of the msl1-msl2 complex (3
Structure deposition date
2012-08-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
9
% buried
8
Peptide accession
Q9HCI7
Residue number A
67
Residue number B
70
Peptide name
E3 ubiquitin-protein ligase MSL2
Ligandability
Cysteine 67 of E3 ubiquitin-protein ligase MSL2
Cysteine 70 of E3 ubiquitin-protein ligase MSL2
4b86 L 62 L 81
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase MSL2 between cysteines 62 and 81.
Details
Redox score ?
75
PDB code
4b86
Structure name
crystal structure of the msl1-msl2 complex (3
Structure deposition date
2012-08-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
7
% buried
nan
Peptide accession
Q9HCI7
Residue number A
62
Residue number B
81
Peptide name
E3 ubiquitin-protein ligase MSL2
Ligandability
Cysteine 62 of E3 ubiquitin-protein ligase MSL2
Cysteine 81 of E3 ubiquitin-protein ligase MSL2
4b86 K 44 K 45
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase MSL2 between cysteines 44 and 45.
Details
Redox score ?
73
PDB code
4b86
Structure name
crystal structure of the msl1-msl2 complex (3
Structure deposition date
2012-08-24
Thiol separation (Å)
6
Half-sphere exposure sum ?
52
Minimum pKa ?
5
% buried
5
Peptide accession
Q9HCI7
Residue number A
44
Residue number B
45
Peptide name
E3 ubiquitin-protein ligase MSL2
Ligandability
Cysteine 44 of E3 ubiquitin-protein ligase MSL2
Cysteine 45 of E3 ubiquitin-protein ligase MSL2
4b86 G 45 G 84
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase MSL2 between cysteines 45 and 84. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
60
PDB code
4b86
Structure name
crystal structure of the msl1-msl2 complex (3
Structure deposition date
2012-08-24
Thiol separation (Å)
7
Half-sphere exposure sum ?
nan
Minimum pKa ?
10
% buried
18
Peptide accession
Q9HCI7
Residue number A
45
Residue number B
84
Peptide name
E3 ubiquitin-protein ligase MSL2
Ligandability
Cysteine 45 of E3 ubiquitin-protein ligase MSL2
Cysteine 84 of E3 ubiquitin-protein ligase MSL2
4b86 L 81 L 84
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase MSL2 between cysteines 81 and 84. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
56
PDB code
4b86
Structure name
crystal structure of the msl1-msl2 complex (3
Structure deposition date
2012-08-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
19
% buried
nan
Peptide accession
Q9HCI7
Residue number A
81
Residue number B
84
Peptide name
E3 ubiquitin-protein ligase MSL2
Ligandability
Cysteine 81 of E3 ubiquitin-protein ligase MSL2
Cysteine 84 of E3 ubiquitin-protein ligase MSL2
4b86 D 45 D 67
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase MSL2 between cysteines 45 and 67. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
4b86
Structure name
crystal structure of the msl1-msl2 complex (3
Structure deposition date
2012-08-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
50
Minimum pKa ?
9
% buried
5
Peptide accession
Q9HCI7
Residue number A
45
Residue number B
67
Peptide name
E3 ubiquitin-protein ligase MSL2
Ligandability
Cysteine 45 of E3 ubiquitin-protein ligase MSL2
Cysteine 67 of E3 ubiquitin-protein ligase MSL2
4b86 C 45 C 62
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase MSL2 between cysteines 45 and 62. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
4b86
Structure name
crystal structure of the msl1-msl2 complex (3
Structure deposition date
2012-08-24
Thiol separation (Å)
8
Half-sphere exposure sum ?
59
Minimum pKa ?
11
% buried
nan
Peptide accession
Q9HCI7
Residue number A
45
Residue number B
62
Peptide name
E3 ubiquitin-protein ligase MSL2
Ligandability
Cysteine 45 of E3 ubiquitin-protein ligase MSL2
Cysteine 62 of E3 ubiquitin-protein ligase MSL2
4b7y C 45 C 70
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase MSL2 between cysteines 45 and 70. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
4b7y
Structure name
crystal structure of the msl1-msl2 complex
Structure deposition date
2012-08-24
Thiol separation (Å)
10
Half-sphere exposure sum ?
61
Minimum pKa ?
10
% buried
32
Peptide accession
Q9HCI7
Residue number A
45
Residue number B
70
Peptide name
E3 ubiquitin-protein ligase MSL2
Ligandability
Cysteine 45 of E3 ubiquitin-protein ligase MSL2
Cysteine 70 of E3 ubiquitin-protein ligase MSL2
4b86 L 45 L 81
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase MSL2 between cysteines 45 and 81. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
4b86
Structure name
crystal structure of the msl1-msl2 complex (3
Structure deposition date
2012-08-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
11
% buried
nan
Peptide accession
Q9HCI7
Residue number A
45
Residue number B
81
Peptide name
E3 ubiquitin-protein ligase MSL2
Ligandability
Cysteine 45 of E3 ubiquitin-protein ligase MSL2
Cysteine 81 of E3 ubiquitin-protein ligase MSL2
4b86 L 45 L 47
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase MSL2 between cysteines 45 and 47. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
35
PDB code
4b86
Structure name
crystal structure of the msl1-msl2 complex (3
Structure deposition date
2012-08-24
Thiol separation (Å)
10
Half-sphere exposure sum ?
60
Minimum pKa ?
11
% buried
33
Peptide accession
Q9HCI7
Residue number A
45
Residue number B
47
Peptide name
E3 ubiquitin-protein ligase MSL2
Ligandability
Cysteine 45 of E3 ubiquitin-protein ligase MSL2
Cysteine 47 of E3 ubiquitin-protein ligase MSL2
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