Protein BUD31 homolog
Intramolecular
Cysteine 134 and cysteine 137
Cysteine 101 and cysteine 142
Cysteine 102 and cysteine 137
Cysteine 101 and cysteine 105
Cysteine 105 and cysteine 119 L
Cysteine 101 and cysteine 119 L
Cysteine 101 and cysteine 139
Cysteine 119 and cysteine 142 L
Cysteine 117 and cysteine 134 L
Cysteine 139 and cysteine 142
More...Cysteine 101 and cysteine 137
Cysteine 134 and cysteine 139
Cysteine 105 and cysteine 142
Cysteine 102 and cysteine 134
Cysteine 101 and cysteine 134
Cysteine 105 and cysteine 117 L
Cysteine 137 and cysteine 139
Cysteine 137 and cysteine 142
Cysteine 117 and cysteine 142 L
Cysteine 119 and cysteine 137 L
Cysteine 105 and cysteine 134
Cysteine 119 and cysteine 134 L
Cysteine 117 and cysteine 119 L
Cysteine 134 and cysteine 142
Cysteine 102 and cysteine 117 L
Cysteine 117 and cysteine 139 L
Cysteine 101 and cysteine 117 L
Cysteine 102 and cysteine 142
Cysteine 117 and cysteine 137 L
Cysteine 102 and cysteine 105
Cysteine 105 and cysteine 137
Cysteine 119 and cysteine 139 L
Cysteine 101 and cysteine 102
Cysteine 105 and cysteine 139
Cysteine 102 and cysteine 139
Cysteine 102 and cysteine 119 L
6ff4 Q 134 Q 137
A redox-regulated disulphide may form within Protein BUD31 homolog between cysteines 134 and 137.
Details
Redox score ?
85
PDB code
6ff4
Structure name
human bact spliceosome core structure
Structure deposition date
2018-01-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
2
% buried
100
Peptide accession
P41223
Residue number A
134
Residue number B
137
Peptide name
Protein BUD31 homolog
Ligandability
Cysteine 134 of Protein BUD31 homolog
Cysteine 137 of Protein BUD31 homolog
7w59 N 101 N 142
A redox-regulated disulphide may form within Protein BUD31 homolog between cysteines 101 and 142.
Details
Redox score ?
84
PDB code
7w59
Structure name
the cryo-em structure of human pre-c*-i complex
Structure deposition date
2021-11-29
Thiol separation (Å)
3
Half-sphere exposure sum ?
77
Minimum pKa ?
3
% buried
100
Peptide accession
P41223
Residue number A
101
Residue number B
142
Peptide name
Protein BUD31 homolog
Ligandability
Cysteine 101 of Protein BUD31 homolog
Cysteine 142 of Protein BUD31 homolog
6ff4 Q 102 Q 137
A redox-regulated disulphide may form within Protein BUD31 homolog between cysteines 102 and 137.
Details
Redox score ?
79
PDB code
6ff4
Structure name
human bact spliceosome core structure
Structure deposition date
2018-01-03
Thiol separation (Å)
3
Half-sphere exposure sum ?
82
Minimum pKa ?
4
% buried
100
Peptide accession
P41223
Residue number A
102
Residue number B
137
Peptide name
Protein BUD31 homolog
Ligandability
Cysteine 102 of Protein BUD31 homolog
Cysteine 137 of Protein BUD31 homolog
6ff4 Q 101 Q 105
A redox-regulated disulphide may form within Protein BUD31 homolog between cysteines 101 and 105.
Details
Redox score ?
74
PDB code
6ff4
Structure name
human bact spliceosome core structure
Structure deposition date
2018-01-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
P41223
Residue number A
101
Residue number B
105
Peptide name
Protein BUD31 homolog
Ligandability
Cysteine 101 of Protein BUD31 homolog
Cysteine 105 of Protein BUD31 homolog
6id1 N 105 N 119
A redox-regulated disulphide may form within Protein BUD31 homolog between cysteines 105 and 119.
Details
Redox score ?
73
PDB code
6id1
Structure name
cryo-em structure of a human intron lariat spliceosome after prp43 loaded (ils2 complex) at 2
Structure deposition date
2018-09-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
P41223
Residue number A
105
Residue number B
119
Peptide name
Protein BUD31 homolog
Ligandability
Cysteine 105 of Protein BUD31 homolog
Cysteine 119 of Protein BUD31 homolog
6icz N 101 N 119
A redox-regulated disulphide may form within Protein BUD31 homolog between cysteines 101 and 119.
Details
Redox score ?
72
PDB code
6icz
Structure name
cryo-em structure of a human post-catalytic spliceosome (p complex) at 3
Structure deposition date
2018-09-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
P41223
Residue number A
101
Residue number B
119
Peptide name
Protein BUD31 homolog
Ligandability
Cysteine 101 of Protein BUD31 homolog
Cysteine 119 of Protein BUD31 homolog
7w59 N 101 N 139
A redox-regulated disulphide may form within Protein BUD31 homolog between cysteines 101 and 139.
Details
Redox score ?
71
PDB code
7w59
Structure name
the cryo-em structure of human pre-c*-i complex
Structure deposition date
2021-11-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
80
Minimum pKa ?
9
% buried
100
Peptide accession
P41223
Residue number A
101
Residue number B
139
Peptide name
Protein BUD31 homolog
Ligandability
Cysteine 101 of Protein BUD31 homolog
Cysteine 139 of Protein BUD31 homolog
6icz N 119 N 142
A redox-regulated disulphide may form within Protein BUD31 homolog between cysteines 119 and 142.
Details
Redox score ?
70
PDB code
6icz
Structure name
cryo-em structure of a human post-catalytic spliceosome (p complex) at 3
Structure deposition date
2018-09-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
11
% buried
nan
Peptide accession
P41223
Residue number A
119
Residue number B
142
Peptide name
Protein BUD31 homolog
Ligandability
Cysteine 119 of Protein BUD31 homolog
Cysteine 142 of Protein BUD31 homolog
6id1 N 117 N 134
A redox-regulated disulphide may form within Protein BUD31 homolog between cysteines 117 and 134.
Details
Redox score ?
69
PDB code
6id1
Structure name
cryo-em structure of a human intron lariat spliceosome after prp43 loaded (ils2 complex) at 2
Structure deposition date
2018-09-07
Thiol separation (Å)
3
Half-sphere exposure sum ?
64
Minimum pKa ?
12
% buried
100
Peptide accession
P41223
Residue number A
117
Residue number B
134
Peptide name
Protein BUD31 homolog
Ligandability
Cysteine 117 of Protein BUD31 homolog
Cysteine 134 of Protein BUD31 homolog
6id1 N 139 N 142
A redox-regulated disulphide may form within Protein BUD31 homolog between cysteines 139 and 142.
Details
Redox score ?
68
PDB code
6id1
Structure name
cryo-em structure of a human intron lariat spliceosome after prp43 loaded (ils2 complex) at 2
Structure deposition date
2018-09-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
11
% buried
100
Peptide accession
P41223
Residue number A
139
Residue number B
142
Peptide name
Protein BUD31 homolog
Ligandability
Cysteine 139 of Protein BUD31 homolog
Cysteine 142 of Protein BUD31 homolog
6id1 N 101 N 137
A redox-regulated disulphide may form within Protein BUD31 homolog between cysteines 101 and 137.
Details
Redox score ?
65
PDB code
6id1
Structure name
cryo-em structure of a human intron lariat spliceosome after prp43 loaded (ils2 complex) at 2
Structure deposition date
2018-09-07
Thiol separation (Å)
3
Half-sphere exposure sum ?
83
Minimum pKa ?
13
% buried
nan
Peptide accession
P41223
Residue number A
101
Residue number B
137
Peptide name
Protein BUD31 homolog
Ligandability
Cysteine 101 of Protein BUD31 homolog
Cysteine 137 of Protein BUD31 homolog
7w59 N 134 N 139
A redox-regulated disulphide may form within Protein BUD31 homolog between cysteines 134 and 139.
Details
Redox score ?
63
PDB code
7w59
Structure name
the cryo-em structure of human pre-c*-i complex
Structure deposition date
2021-11-29
Thiol separation (Å)
7
Half-sphere exposure sum ?
63
Minimum pKa ?
6
% buried
100
Peptide accession
P41223
Residue number A
134
Residue number B
139
Peptide name
Protein BUD31 homolog
Ligandability
Cysteine 134 of Protein BUD31 homolog
Cysteine 139 of Protein BUD31 homolog
6id0 N 105 N 142
A redox-regulated disulphide may form within Protein BUD31 homolog between cysteines 105 and 142. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
58
PDB code
6id0
Structure name
cryo-em structure of a human intron lariat spliceosome prior to prp43 loaded (ils1 complex) at 2
Structure deposition date
2018-09-07
Thiol separation (Å)
6
Half-sphere exposure sum ?
71
Minimum pKa ?
11
% buried
nan
Peptide accession
P41223
Residue number A
105
Residue number B
142
Peptide name
Protein BUD31 homolog
Ligandability
Cysteine 105 of Protein BUD31 homolog
Cysteine 142 of Protein BUD31 homolog
7w59 N 102 N 134
A redox-regulated disulphide may form within Protein BUD31 homolog between cysteines 102 and 134. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
56
PDB code
7w59
Structure name
the cryo-em structure of human pre-c*-i complex
Structure deposition date
2021-11-29
Thiol separation (Å)
7
Half-sphere exposure sum ?
72
Minimum pKa ?
6
% buried
100
Peptide accession
P41223
Residue number A
102
Residue number B
134
Peptide name
Protein BUD31 homolog
Ligandability
Cysteine 102 of Protein BUD31 homolog
Cysteine 134 of Protein BUD31 homolog
7w59 N 101 N 134
A redox-regulated disulphide may form within Protein BUD31 homolog between cysteines 101 and 134. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
56
PDB code
7w59
Structure name
the cryo-em structure of human pre-c*-i complex
Structure deposition date
2021-11-29
Thiol separation (Å)
7
Half-sphere exposure sum ?
74
Minimum pKa ?
6
% buried
100
Peptide accession
P41223
Residue number A
101
Residue number B
134
Peptide name
Protein BUD31 homolog
Ligandability
Cysteine 101 of Protein BUD31 homolog
Cysteine 134 of Protein BUD31 homolog
6ff4 Q 105 Q 117
A redox-regulated disulphide may form within Protein BUD31 homolog between cysteines 105 and 117. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
55
PDB code
6ff4
Structure name
human bact spliceosome core structure
Structure deposition date
2018-01-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
19
% buried
nan
Peptide accession
P41223
Residue number A
105
Residue number B
117
Peptide name
Protein BUD31 homolog
Ligandability
Cysteine 105 of Protein BUD31 homolog
Cysteine 117 of Protein BUD31 homolog
7w5a N 137 N 139
A redox-regulated disulphide may form within Protein BUD31 homolog between cysteines 137 and 139. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
53
PDB code
7w5a
Structure name
the cryo-em structure of human pre-c*-ii complex
Structure deposition date
2021-11-29
Thiol separation (Å)
6
Half-sphere exposure sum ?
71
Minimum pKa ?
13
% buried
100
Peptide accession
P41223
Residue number A
137
Residue number B
139
Peptide name
Protein BUD31 homolog
Ligandability
Cysteine 137 of Protein BUD31 homolog
Cysteine 139 of Protein BUD31 homolog
6id1 N 137 N 142
A redox-regulated disulphide may form within Protein BUD31 homolog between cysteines 137 and 142. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
6id1
Structure name
cryo-em structure of a human intron lariat spliceosome after prp43 loaded (ils2 complex) at 2
Structure deposition date
2018-09-07
Thiol separation (Å)
7
Half-sphere exposure sum ?
68
Minimum pKa ?
11
% buried
100
Peptide accession
P41223
Residue number A
137
Residue number B
142
Peptide name
Protein BUD31 homolog
Ligandability
Cysteine 137 of Protein BUD31 homolog
Cysteine 142 of Protein BUD31 homolog
6id1 N 117 N 142
A redox-regulated disulphide may form within Protein BUD31 homolog between cysteines 117 and 142. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
6id1
Structure name
cryo-em structure of a human intron lariat spliceosome after prp43 loaded (ils2 complex) at 2
Structure deposition date
2018-09-07
Thiol separation (Å)
7
Half-sphere exposure sum ?
66
Minimum pKa ?
11
% buried
100
Peptide accession
P41223
Residue number A
117
Residue number B
142
Peptide name
Protein BUD31 homolog
Ligandability
Cysteine 117 of Protein BUD31 homolog
Cysteine 142 of Protein BUD31 homolog
6ff4 Q 119 Q 137
A redox-regulated disulphide may form within Protein BUD31 homolog between cysteines 119 and 137. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
6ff4
Structure name
human bact spliceosome core structure
Structure deposition date
2018-01-03
Thiol separation (Å)
6
Half-sphere exposure sum ?
66
Minimum pKa ?
13
% buried
100
Peptide accession
P41223
Residue number A
119
Residue number B
137
Peptide name
Protein BUD31 homolog
Ligandability
Cysteine 119 of Protein BUD31 homolog
Cysteine 137 of Protein BUD31 homolog
6icz N 105 N 134
A redox-regulated disulphide may form within Protein BUD31 homolog between cysteines 105 and 134. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
6icz
Structure name
cryo-em structure of a human post-catalytic spliceosome (p complex) at 3
Structure deposition date
2018-09-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
23
% buried
nan
Peptide accession
P41223
Residue number A
105
Residue number B
134
Peptide name
Protein BUD31 homolog
Ligandability
Cysteine 105 of Protein BUD31 homolog
Cysteine 134 of Protein BUD31 homolog
6icz N 119 N 134
A redox-regulated disulphide may form within Protein BUD31 homolog between cysteines 119 and 134. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
6icz
Structure name
cryo-em structure of a human post-catalytic spliceosome (p complex) at 3
Structure deposition date
2018-09-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
23
% buried
nan
Peptide accession
P41223
Residue number A
119
Residue number B
134
Peptide name
Protein BUD31 homolog
Ligandability
Cysteine 119 of Protein BUD31 homolog
Cysteine 134 of Protein BUD31 homolog
6id0 N 117 N 119
A redox-regulated disulphide may form within Protein BUD31 homolog between cysteines 117 and 119. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
6id0
Structure name
cryo-em structure of a human intron lariat spliceosome prior to prp43 loaded (ils1 complex) at 2
Structure deposition date
2018-09-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
23
% buried
nan
Peptide accession
P41223
Residue number A
117
Residue number B
119
Peptide name
Protein BUD31 homolog
Ligandability
Cysteine 117 of Protein BUD31 homolog
Cysteine 119 of Protein BUD31 homolog
6icz N 134 N 142
A redox-regulated disulphide may form within Protein BUD31 homolog between cysteines 134 and 142. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
6icz
Structure name
cryo-em structure of a human post-catalytic spliceosome (p complex) at 3
Structure deposition date
2018-09-07
Thiol separation (Å)
8
Half-sphere exposure sum ?
64
Minimum pKa ?
11
% buried
100
Peptide accession
P41223
Residue number A
134
Residue number B
142
Peptide name
Protein BUD31 homolog
Ligandability
Cysteine 134 of Protein BUD31 homolog
Cysteine 142 of Protein BUD31 homolog
6ff4 Q 102 Q 117
A redox-regulated disulphide may form within Protein BUD31 homolog between cysteines 102 and 117. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
6ff4
Structure name
human bact spliceosome core structure
Structure deposition date
2018-01-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
77
Minimum pKa ?
4
% buried
100
Peptide accession
P41223
Residue number A
102
Residue number B
117
Peptide name
Protein BUD31 homolog
Ligandability
Cysteine 102 of Protein BUD31 homolog
Cysteine 117 of Protein BUD31 homolog
6icz N 117 N 139
A redox-regulated disulphide may form within Protein BUD31 homolog between cysteines 117 and 139. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
6icz
Structure name
cryo-em structure of a human post-catalytic spliceosome (p complex) at 3
Structure deposition date
2018-09-07
Thiol separation (Å)
7
Half-sphere exposure sum ?
70
Minimum pKa ?
13
% buried
100
Peptide accession
P41223
Residue number A
117
Residue number B
139
Peptide name
Protein BUD31 homolog
Ligandability
Cysteine 117 of Protein BUD31 homolog
Cysteine 139 of Protein BUD31 homolog
7w59 N 101 N 117
A redox-regulated disulphide may form within Protein BUD31 homolog between cysteines 101 and 117. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
7w59
Structure name
the cryo-em structure of human pre-c*-i complex
Structure deposition date
2021-11-29
Thiol separation (Å)
8
Half-sphere exposure sum ?
79
Minimum pKa ?
9
% buried
100
Peptide accession
P41223
Residue number A
101
Residue number B
117
Peptide name
Protein BUD31 homolog
Ligandability
Cysteine 101 of Protein BUD31 homolog
Cysteine 117 of Protein BUD31 homolog
6id1 N 102 N 142
A redox-regulated disulphide may form within Protein BUD31 homolog between cysteines 102 and 142. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
6id1
Structure name
cryo-em structure of a human intron lariat spliceosome after prp43 loaded (ils2 complex) at 2
Structure deposition date
2018-09-07
Thiol separation (Å)
7
Half-sphere exposure sum ?
80
Minimum pKa ?
11
% buried
100
Peptide accession
P41223
Residue number A
102
Residue number B
142
Peptide name
Protein BUD31 homolog
Ligandability
Cysteine 102 of Protein BUD31 homolog
Cysteine 142 of Protein BUD31 homolog
6id1 N 117 N 137
A redox-regulated disulphide may form within Protein BUD31 homolog between cysteines 117 and 137. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
6id1
Structure name
cryo-em structure of a human intron lariat spliceosome after prp43 loaded (ils2 complex) at 2
Structure deposition date
2018-09-07
Thiol separation (Å)
7
Half-sphere exposure sum ?
70
Minimum pKa ?
13
% buried
100
Peptide accession
P41223
Residue number A
117
Residue number B
137
Peptide name
Protein BUD31 homolog
Ligandability
Cysteine 117 of Protein BUD31 homolog
Cysteine 137 of Protein BUD31 homolog
6icz N 102 N 105
A redox-regulated disulphide may form within Protein BUD31 homolog between cysteines 102 and 105. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
6icz
Structure name
cryo-em structure of a human post-catalytic spliceosome (p complex) at 3
Structure deposition date
2018-09-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
86
Minimum pKa ?
24
% buried
nan
Peptide accession
P41223
Residue number A
102
Residue number B
105
Peptide name
Protein BUD31 homolog
Ligandability
Cysteine 102 of Protein BUD31 homolog
Cysteine 105 of Protein BUD31 homolog
6ff4 Q 105 Q 137
A redox-regulated disulphide may form within Protein BUD31 homolog between cysteines 105 and 137. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
6ff4
Structure name
human bact spliceosome core structure
Structure deposition date
2018-01-03
Thiol separation (Å)
3
Half-sphere exposure sum ?
68
Minimum pKa ?
27
% buried
nan
Peptide accession
P41223
Residue number A
105
Residue number B
137
Peptide name
Protein BUD31 homolog
Ligandability
Cysteine 105 of Protein BUD31 homolog
Cysteine 137 of Protein BUD31 homolog
6id0 N 119 N 139
A redox-regulated disulphide may form within Protein BUD31 homolog between cysteines 119 and 139. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
6id0
Structure name
cryo-em structure of a human intron lariat spliceosome prior to prp43 loaded (ils1 complex) at 2
Structure deposition date
2018-09-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
28
% buried
nan
Peptide accession
P41223
Residue number A
119
Residue number B
139
Peptide name
Protein BUD31 homolog
Ligandability
Cysteine 119 of Protein BUD31 homolog
Cysteine 139 of Protein BUD31 homolog
6id1 N 101 N 102
A redox-regulated disulphide may form within Protein BUD31 homolog between cysteines 101 and 102. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
6id1
Structure name
cryo-em structure of a human intron lariat spliceosome after prp43 loaded (ils2 complex) at 2
Structure deposition date
2018-09-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
95
Minimum pKa ?
25
% buried
nan
Peptide accession
P41223
Residue number A
101
Residue number B
102
Peptide name
Protein BUD31 homolog
Ligandability
Cysteine 101 of Protein BUD31 homolog
Cysteine 102 of Protein BUD31 homolog
6id1 N 105 N 139
A redox-regulated disulphide may form within Protein BUD31 homolog between cysteines 105 and 139. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
30
PDB code
6id1
Structure name
cryo-em structure of a human intron lariat spliceosome after prp43 loaded (ils2 complex) at 2
Structure deposition date
2018-09-07
Thiol separation (Å)
6
Half-sphere exposure sum ?
70
Minimum pKa ?
23
% buried
nan
Peptide accession
P41223
Residue number A
105
Residue number B
139
Peptide name
Protein BUD31 homolog
Ligandability
Cysteine 105 of Protein BUD31 homolog
Cysteine 139 of Protein BUD31 homolog
7w5a N 102 N 139
A redox-regulated disulphide may form within Protein BUD31 homolog between cysteines 102 and 139. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
26
PDB code
7w5a
Structure name
the cryo-em structure of human pre-c*-ii complex
Structure deposition date
2021-11-29
Thiol separation (Å)
8
Half-sphere exposure sum ?
78
Minimum pKa ?
17
% buried
100
Peptide accession
P41223
Residue number A
102
Residue number B
139
Peptide name
Protein BUD31 homolog
Ligandability
Cysteine 102 of Protein BUD31 homolog
Cysteine 139 of Protein BUD31 homolog
6icz N 102 N 119
A redox-regulated disulphide may form within Protein BUD31 homolog between cysteines 102 and 119. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
23
PDB code
6icz
Structure name
cryo-em structure of a human post-catalytic spliceosome (p complex) at 3
Structure deposition date
2018-09-07
Thiol separation (Å)
7
Half-sphere exposure sum ?
83
Minimum pKa ?
24
% buried
nan
Peptide accession
P41223
Residue number A
102
Residue number B
119
Peptide name
Protein BUD31 homolog
Ligandability
Cysteine 102 of Protein BUD31 homolog
Cysteine 119 of Protein BUD31 homolog
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