Protein AF-10
Intramolecular
Cysteine 137 and cysteine 140
Cysteine 42 and cysteine 47
Cysteine 137 and cysteine 170
Cysteine 157 and cysteine 162
Cysteine 42 and cysteine 71
Cysteine 47 and cysteine 71
Cysteine 82 and cysteine 85
Cysteine 42 and cysteine 68
Cysteine 47 and cysteine 68
Cysteine 137 and cysteine 154
More...Cysteine 162 and cysteine 194
Cysteine 157 and cysteine 194
Cysteine 85 and cysteine 105
Cysteine 68 and cysteine 71
Cysteine 82 and cysteine 105
Cysteine 140 and cysteine 170
Cysteine 178 and cysteine 191
Cysteine 28 and cysteine 55
Cysteine 25 and cysteine 28
Cysteine 25 and cysteine 26
Cysteine 85 and cysteine 137
Cysteine 26 and cysteine 47
Cysteine 25 and cysteine 55
Cysteine 26 and cysteine 42
Cysteine 157 and cysteine 191
Cysteine 140 and cysteine 154
Cysteine 85 and cysteine 170
Cysteine 85 and cysteine 140
Cysteine 157 and cysteine 178
Cysteine 26 and cysteine 68
Cysteine 154 and cysteine 170
Cysteine 26 and cysteine 55
Cysteine 26 and cysteine 28
Cysteine 85 and cysteine 154
Cysteine 105 and cysteine 154
Cysteine 105 and cysteine 170
7mju A 137 A 140
A redox-regulated disulphide may form within Protein AF-10 between cysteines 137 and 140.
Details
Redox score ?
91
PDB code
7mju
Structure name
crystal structure of human af10 pzp bound to histone h3 tail
Structure deposition date
2021-04-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
2
% buried
44
Peptide accession
P55197
Residue number A
137
Residue number B
140
Peptide name
Protein AF-10
Ligandability
Cysteine 137 of Protein AF-10
Cysteine 140 of Protein AF-10
7mju A 42 A 47
A redox-regulated disulphide may form within Protein AF-10 between cysteines 42 and 47.
Details
Redox score ?
86
PDB code
7mju
Structure name
crystal structure of human af10 pzp bound to histone h3 tail
Structure deposition date
2021-04-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
7
% buried
40
Peptide accession
P55197
Residue number A
42
Residue number B
47
Peptide name
Protein AF-10
Ligandability
Cysteine 42 of Protein AF-10
Cysteine 47 of Protein AF-10
7mju A 137 A 170
A redox-regulated disulphide may form within Protein AF-10 between cysteines 137 and 170.
Details
Redox score ?
86
PDB code
7mju
Structure name
crystal structure of human af10 pzp bound to histone h3 tail
Structure deposition date
2021-04-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
77
Minimum pKa ?
2
% buried
60
Peptide accession
P55197
Residue number A
137
Residue number B
170
Peptide name
Protein AF-10
Ligandability
Cysteine 137 of Protein AF-10
Cysteine 170 of Protein AF-10
5dah B 157 B 162
A redox-regulated disulphide may form within Protein AF-10 between cysteines 157 and 162.
Details
Redox score ?
85
PDB code
5dah
Structure name
crystal structure of pzp domain of human af10 protein fused with histone h3 peptide
Structure deposition date
2015-08-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
7
% buried
24
Peptide accession
P55197
Residue number A
157
Residue number B
162
Peptide name
Protein AF-10
Ligandability
Cysteine 157 of Protein AF-10
Cysteine 162 of Protein AF-10
5dah A 42 A 71
A redox-regulated disulphide may form within Protein AF-10 between cysteines 42 and 71.
Details
Redox score ?
83
PDB code
5dah
Structure name
crystal structure of pzp domain of human af10 protein fused with histone h3 peptide
Structure deposition date
2015-08-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
7
% buried
27
Peptide accession
P55197
Residue number A
42
Residue number B
71
Peptide name
Protein AF-10
Ligandability
Cysteine 42 of Protein AF-10
Cysteine 71 of Protein AF-10
5dah B 47 B 71
A redox-regulated disulphide may form within Protein AF-10 between cysteines 47 and 71.
Details
Redox score ?
81
PDB code
5dah
Structure name
crystal structure of pzp domain of human af10 protein fused with histone h3 peptide
Structure deposition date
2015-08-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
9
% buried
28
Peptide accession
P55197
Residue number A
47
Residue number B
71
Peptide name
Protein AF-10
Ligandability
Cysteine 47 of Protein AF-10
Cysteine 71 of Protein AF-10
7mju A 82 A 85
A redox-regulated disulphide may form within Protein AF-10 between cysteines 82 and 85.
Details
Redox score ?
81
PDB code
7mju
Structure name
crystal structure of human af10 pzp bound to histone h3 tail
Structure deposition date
2021-04-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
79
Minimum pKa ?
5
% buried
nan
Peptide accession
P55197
Residue number A
82
Residue number B
85
Peptide name
Protein AF-10
Ligandability
Cysteine 82 of Protein AF-10
Cysteine 85 of Protein AF-10
5dah B 42 B 68
A redox-regulated disulphide may form within Protein AF-10 between cysteines 42 and 68.
Details
Redox score ?
79
PDB code
5dah
Structure name
crystal structure of pzp domain of human af10 protein fused with histone h3 peptide
Structure deposition date
2015-08-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
7
% buried
46
Peptide accession
P55197
Residue number A
42
Residue number B
68
Peptide name
Protein AF-10
Ligandability
Cysteine 42 of Protein AF-10
Cysteine 68 of Protein AF-10
5dah A 47 A 68
A redox-regulated disulphide may form within Protein AF-10 between cysteines 47 and 68.
Details
Redox score ?
79
PDB code
5dah
Structure name
crystal structure of pzp domain of human af10 protein fused with histone h3 peptide
Structure deposition date
2015-08-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
9
% buried
53
Peptide accession
P55197
Residue number A
47
Residue number B
68
Peptide name
Protein AF-10
Ligandability
Cysteine 47 of Protein AF-10
Cysteine 68 of Protein AF-10
5dag A 137 A 154
A redox-regulated disulphide may form within Protein AF-10 between cysteines 137 and 154.
Details
Redox score ?
79
PDB code
5dag
Structure name
crystal structure of pzp domain of human af10 protein
Structure deposition date
2015-08-19
Thiol separation (Å)
5
Half-sphere exposure sum ?
83
Minimum pKa ?
2
% buried
66
Peptide accession
P55197
Residue number A
137
Residue number B
154
Peptide name
Protein AF-10
Ligandability
Cysteine 137 of Protein AF-10
Cysteine 154 of Protein AF-10
5dah A 162 A 194
A redox-regulated disulphide may form within Protein AF-10 between cysteines 162 and 194.
Details
Redox score ?
75
PDB code
5dah
Structure name
crystal structure of pzp domain of human af10 protein fused with histone h3 peptide
Structure deposition date
2015-08-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
9
% buried
34
Peptide accession
P55197
Residue number A
162
Residue number B
194
Peptide name
Protein AF-10
Ligandability
Cysteine 162 of Protein AF-10
Cysteine 194 of Protein AF-10
7mju A 157 A 194
A redox-regulated disulphide may form within Protein AF-10 between cysteines 157 and 194.
Details
Redox score ?
74
PDB code
7mju
Structure name
crystal structure of human af10 pzp bound to histone h3 tail
Structure deposition date
2021-04-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
67
Minimum pKa ?
9
% buried
21
Peptide accession
P55197
Residue number A
157
Residue number B
194
Peptide name
Protein AF-10
Ligandability
Cysteine 157 of Protein AF-10
Cysteine 194 of Protein AF-10
7mju A 85 A 105
A redox-regulated disulphide may form within Protein AF-10 between cysteines 85 and 105.
Details
Redox score ?
74
PDB code
7mju
Structure name
crystal structure of human af10 pzp bound to histone h3 tail
Structure deposition date
2021-04-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
90
Minimum pKa ?
5
% buried
92
Peptide accession
P55197
Residue number A
85
Residue number B
105
Peptide name
Protein AF-10
Ligandability
Cysteine 85 of Protein AF-10
Cysteine 105 of Protein AF-10
5dah A 68 A 71
A redox-regulated disulphide may form within Protein AF-10 between cysteines 68 and 71.
Details
Redox score ?
74
PDB code
5dah
Structure name
crystal structure of pzp domain of human af10 protein fused with histone h3 peptide
Structure deposition date
2015-08-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
10
% buried
42
Peptide accession
P55197
Residue number A
68
Residue number B
71
Peptide name
Protein AF-10
Ligandability
Cysteine 68 of Protein AF-10
Cysteine 71 of Protein AF-10
5dah A 82 A 105
A redox-regulated disulphide may form within Protein AF-10 between cysteines 82 and 105.
Details
Redox score ?
74
PDB code
5dah
Structure name
crystal structure of pzp domain of human af10 protein fused with histone h3 peptide
Structure deposition date
2015-08-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
83
Minimum pKa ?
6
% buried
98
Peptide accession
P55197
Residue number A
82
Residue number B
105
Peptide name
Protein AF-10
Ligandability
Cysteine 82 of Protein AF-10
Cysteine 105 of Protein AF-10
7mju A 140 A 170
A redox-regulated disulphide may form within Protein AF-10 between cysteines 140 and 170.
Details
Redox score ?
72
PDB code
7mju
Structure name
crystal structure of human af10 pzp bound to histone h3 tail
Structure deposition date
2021-04-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
9
% buried
47
Peptide accession
P55197
Residue number A
140
Residue number B
170
Peptide name
Protein AF-10
Ligandability
Cysteine 140 of Protein AF-10
Cysteine 170 of Protein AF-10
5dah B 178 B 191
A redox-regulated disulphide may form within Protein AF-10 between cysteines 178 and 191.
Details
Redox score ?
69
PDB code
5dah
Structure name
crystal structure of pzp domain of human af10 protein fused with histone h3 peptide
Structure deposition date
2015-08-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
8
% buried
55
Peptide accession
P55197
Residue number A
178
Residue number B
191
Peptide name
Protein AF-10
Ligandability
Cysteine 178 of Protein AF-10
Cysteine 191 of Protein AF-10
7mju A 28 A 55
A redox-regulated disulphide may form within Protein AF-10 between cysteines 28 and 55.
Details
Redox score ?
67
PDB code
7mju
Structure name
crystal structure of human af10 pzp bound to histone h3 tail
Structure deposition date
2021-04-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
10
% buried
58
Peptide accession
P55197
Residue number A
28
Residue number B
55
Peptide name
Protein AF-10
Ligandability
Cysteine 28 of Protein AF-10
Cysteine 55 of Protein AF-10
5dah A 25 A 28
A redox-regulated disulphide may form within Protein AF-10 between cysteines 25 and 28.
Details
Redox score ?
65
PDB code
5dah
Structure name
crystal structure of pzp domain of human af10 protein fused with histone h3 peptide
Structure deposition date
2015-08-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
78
Minimum pKa ?
10
% buried
nan
Peptide accession
P55197
Residue number A
25
Residue number B
28
Peptide name
Protein AF-10
Ligandability
Cysteine 25 of Protein AF-10
Cysteine 28 of Protein AF-10
5dah A 25 A 26
A redox-regulated disulphide may form within Protein AF-10 between cysteines 25 and 26. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
56
PDB code
5dah
Structure name
crystal structure of pzp domain of human af10 protein fused with histone h3 peptide
Structure deposition date
2015-08-19
Thiol separation (Å)
6
Half-sphere exposure sum ?
73
Minimum pKa ?
12
% buried
nan
Peptide accession
P55197
Residue number A
25
Residue number B
26
Peptide name
Protein AF-10
Ligandability
Cysteine 25 of Protein AF-10
Cysteine 26 of Protein AF-10
7mju A 85 A 137
A redox-regulated disulphide may form within Protein AF-10 between cysteines 85 and 137. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
56
PDB code
7mju
Structure name
crystal structure of human af10 pzp bound to histone h3 tail
Structure deposition date
2021-04-20
Thiol separation (Å)
9
Half-sphere exposure sum ?
81
Minimum pKa ?
2
% buried
70
Peptide accession
P55197
Residue number A
85
Residue number B
137
Peptide name
Protein AF-10
Ligandability
Cysteine 85 of Protein AF-10
Cysteine 137 of Protein AF-10
5dah B 26 B 47
A redox-regulated disulphide may form within Protein AF-10 between cysteines 26 and 47. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
5dah
Structure name
crystal structure of pzp domain of human af10 protein fused with histone h3 peptide
Structure deposition date
2015-08-19
Thiol separation (Å)
8
Half-sphere exposure sum ?
64
Minimum pKa ?
9
% buried
68
Peptide accession
P55197
Residue number A
26
Residue number B
47
Peptide name
Protein AF-10
Ligandability
Cysteine 26 of Protein AF-10
Cysteine 47 of Protein AF-10
5dah A 25 A 55
A redox-regulated disulphide may form within Protein AF-10 between cysteines 25 and 55. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
5dah
Structure name
crystal structure of pzp domain of human af10 protein fused with histone h3 peptide
Structure deposition date
2015-08-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
80
Minimum pKa ?
19
% buried
nan
Peptide accession
P55197
Residue number A
25
Residue number B
55
Peptide name
Protein AF-10
Ligandability
Cysteine 25 of Protein AF-10
Cysteine 55 of Protein AF-10
7mju A 26 A 42
A redox-regulated disulphide may form within Protein AF-10 between cysteines 26 and 42. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
7mju
Structure name
crystal structure of human af10 pzp bound to histone h3 tail
Structure deposition date
2021-04-20
Thiol separation (Å)
9
Half-sphere exposure sum ?
68
Minimum pKa ?
7
% buried
55
Peptide accession
P55197
Residue number A
26
Residue number B
42
Peptide name
Protein AF-10
Ligandability
Cysteine 26 of Protein AF-10
Cysteine 42 of Protein AF-10
7mju A 157 A 191
A redox-regulated disulphide may form within Protein AF-10 between cysteines 157 and 191. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
7mju
Structure name
crystal structure of human af10 pzp bound to histone h3 tail
Structure deposition date
2021-04-20
Thiol separation (Å)
9
Half-sphere exposure sum ?
61
Minimum pKa ?
9
% buried
25
Peptide accession
P55197
Residue number A
157
Residue number B
191
Peptide name
Protein AF-10
Ligandability
Cysteine 157 of Protein AF-10
Cysteine 191 of Protein AF-10
5dah A 140 A 154
A redox-regulated disulphide may form within Protein AF-10 between cysteines 140 and 154. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
5dah
Structure name
crystal structure of pzp domain of human af10 protein fused with histone h3 peptide
Structure deposition date
2015-08-19
Thiol separation (Å)
8
Half-sphere exposure sum ?
81
Minimum pKa ?
10
% buried
62
Peptide accession
P55197
Residue number A
140
Residue number B
154
Peptide name
Protein AF-10
Ligandability
Cysteine 140 of Protein AF-10
Cysteine 154 of Protein AF-10
5dag A 85 A 170
A redox-regulated disulphide may form within Protein AF-10 between cysteines 85 and 170. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
5dag
Structure name
crystal structure of pzp domain of human af10 protein
Structure deposition date
2015-08-19
Thiol separation (Å)
7
Half-sphere exposure sum ?
79
Minimum pKa ?
15
% buried
nan
Peptide accession
P55197
Residue number A
85
Residue number B
170
Peptide name
Protein AF-10
Ligandability
Cysteine 85 of Protein AF-10
Cysteine 170 of Protein AF-10
5dah A 85 A 140
A redox-regulated disulphide may form within Protein AF-10 between cysteines 85 and 140. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
5dah
Structure name
crystal structure of pzp domain of human af10 protein fused with histone h3 peptide
Structure deposition date
2015-08-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
10
% buried
nan
Peptide accession
P55197
Residue number A
85
Residue number B
140
Peptide name
Protein AF-10
Ligandability
Cysteine 85 of Protein AF-10
Cysteine 140 of Protein AF-10
5dah B 157 B 178
A redox-regulated disulphide may form within Protein AF-10 between cysteines 157 and 178. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
5dah
Structure name
crystal structure of pzp domain of human af10 protein fused with histone h3 peptide
Structure deposition date
2015-08-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
61
Minimum pKa ?
8
% buried
47
Peptide accession
P55197
Residue number A
157
Residue number B
178
Peptide name
Protein AF-10
Ligandability
Cysteine 157 of Protein AF-10
Cysteine 178 of Protein AF-10
5dah B 26 B 68
A redox-regulated disulphide may form within Protein AF-10 between cysteines 26 and 68. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
5dah
Structure name
crystal structure of pzp domain of human af10 protein fused with histone h3 peptide
Structure deposition date
2015-08-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
72
Minimum pKa ?
10
% buried
80
Peptide accession
P55197
Residue number A
26
Residue number B
68
Peptide name
Protein AF-10
Ligandability
Cysteine 26 of Protein AF-10
Cysteine 68 of Protein AF-10
5dag A 154 A 170
A redox-regulated disulphide may form within Protein AF-10 between cysteines 154 and 170. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
5dag
Structure name
crystal structure of pzp domain of human af10 protein
Structure deposition date
2015-08-19
Thiol separation (Å)
8
Half-sphere exposure sum ?
84
Minimum pKa ?
12
% buried
67
Peptide accession
P55197
Residue number A
154
Residue number B
170
Peptide name
Protein AF-10
Ligandability
Cysteine 154 of Protein AF-10
Cysteine 170 of Protein AF-10
5dah A 26 A 55
A redox-regulated disulphide may form within Protein AF-10 between cysteines 26 and 55. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
5dah
Structure name
crystal structure of pzp domain of human af10 protein fused with histone h3 peptide
Structure deposition date
2015-08-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
81
Minimum pKa ?
12
% buried
94
Peptide accession
P55197
Residue number A
26
Residue number B
55
Peptide name
Protein AF-10
Ligandability
Cysteine 26 of Protein AF-10
Cysteine 55 of Protein AF-10
5dah A 26 A 28
A redox-regulated disulphide may form within Protein AF-10 between cysteines 26 and 28. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
5dah
Structure name
crystal structure of pzp domain of human af10 protein fused with histone h3 peptide
Structure deposition date
2015-08-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
79
Minimum pKa ?
10
% buried
88
Peptide accession
P55197
Residue number A
26
Residue number B
28
Peptide name
Protein AF-10
Ligandability
Cysteine 26 of Protein AF-10
Cysteine 28 of Protein AF-10
5dag A 85 A 154
A redox-regulated disulphide may form within Protein AF-10 between cysteines 85 and 154. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
31
PDB code
5dag
Structure name
crystal structure of pzp domain of human af10 protein
Structure deposition date
2015-08-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
85
Minimum pKa ?
12
% buried
nan
Peptide accession
P55197
Residue number A
85
Residue number B
154
Peptide name
Protein AF-10
Ligandability
Cysteine 85 of Protein AF-10
Cysteine 154 of Protein AF-10
5dag A 105 A 154
A redox-regulated disulphide may form within Protein AF-10 between cysteines 105 and 154. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
26
PDB code
5dag
Structure name
crystal structure of pzp domain of human af10 protein
Structure deposition date
2015-08-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
91
Minimum pKa ?
12
% buried
88
Peptide accession
P55197
Residue number A
105
Residue number B
154
Peptide name
Protein AF-10
Ligandability
Cysteine 105 of Protein AF-10
Cysteine 154 of Protein AF-10
5dah A 105 A 170
A redox-regulated disulphide may form within Protein AF-10 between cysteines 105 and 170. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
15
PDB code
5dah
Structure name
crystal structure of pzp domain of human af10 protein fused with histone h3 peptide
Structure deposition date
2015-08-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
89
Minimum pKa ?
19
% buried
91
Peptide accession
P55197
Residue number A
105
Residue number B
170
Peptide name
Protein AF-10
Ligandability
Cysteine 105 of Protein AF-10
Cysteine 170 of Protein AF-10
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