Tumor necrosis factor receptor superfamily member 11B
Intramolecular
Cysteine 65 and cysteine 80
Cysteine 166 and cysteine 185
Cysteine 124 and cysteine 142
Cysteine 83 and cysteine 97
Cysteine 145 and cysteine 160
Cysteine 107 and cysteine 118
Cysteine 87 and cysteine 105
Cysteine 41 and cysteine 54
Cysteine 44 and cysteine 62
Cysteine 124 and cysteine 160
More...Cysteine 124 and cysteine 145
Cysteine 65 and cysteine 83
Cysteine 142 and cysteine 160
Cysteine 87 and cysteine 118
Cysteine 80 and cysteine 83
Cysteine 142 and cysteine 145
Cysteine 44 and cysteine 80
Cysteine 105 and cysteine 118
Cysteine 65 and cysteine 97
Cysteine 41 and cysteine 62
Cysteine 44 and cysteine 65
Cysteine 87 and cysteine 107
Cysteine 105 and cysteine 107
Cysteine 54 and cysteine 62
Cysteine 80 and cysteine 97
Cysteine 41 and cysteine 44
Cysteine 44 and cysteine 54
3urf Z 44 Z 59
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 11B between cysteines 65 and 80 (44 and 59 respectively in this structure).
Details
Redox score ?
89
PDB code
3urf
Structure name
human rankl/opg complex
Structure deposition date
2011-11-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
O00300
Residue number A
65
Residue number B
80
Peptide name
Tumor necrosis factor receptor superfamily member 11B
Ligandability
Cysteine 65 of Tumor necrosis factor receptor superfamily member 11B
Cysteine 80 of Tumor necrosis factor receptor superfamily member 11B
3urf Z 145 Z 164
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 11B between cysteines 166 and 185 (145 and 164 respectively in this structure).
Details
Redox score ?
88
PDB code
3urf
Structure name
human rankl/opg complex
Structure deposition date
2011-11-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
46
Minimum pKa ?
nan
% buried
nan
Peptide accession
O00300
Residue number A
166
Residue number B
185
Peptide name
Tumor necrosis factor receptor superfamily member 11B
Ligandability
Cysteine 166 of Tumor necrosis factor receptor superfamily member 11B
Cysteine 185 of Tumor necrosis factor receptor superfamily member 11B
3urf Z 103 Z 121
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 11B between cysteines 124 and 142 (103 and 121 respectively in this structure).
Details
Redox score ?
88
PDB code
3urf
Structure name
human rankl/opg complex
Structure deposition date
2011-11-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
O00300
Residue number A
124
Residue number B
142
Peptide name
Tumor necrosis factor receptor superfamily member 11B
Ligandability
Cysteine 124 of Tumor necrosis factor receptor superfamily member 11B
Cysteine 142 of Tumor necrosis factor receptor superfamily member 11B
3urf Z 62 Z 76
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 11B between cysteines 83 and 97 (62 and 76 respectively in this structure).
Details
Redox score ?
88
PDB code
3urf
Structure name
human rankl/opg complex
Structure deposition date
2011-11-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
O00300
Residue number A
83
Residue number B
97
Peptide name
Tumor necrosis factor receptor superfamily member 11B
Ligandability
Cysteine 83 of Tumor necrosis factor receptor superfamily member 11B
Cysteine 97 of Tumor necrosis factor receptor superfamily member 11B
3urf Z 124 Z 139
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 11B between cysteines 145 and 160 (124 and 139 respectively in this structure).
Details
Redox score ?
88
PDB code
3urf
Structure name
human rankl/opg complex
Structure deposition date
2011-11-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
O00300
Residue number A
145
Residue number B
160
Peptide name
Tumor necrosis factor receptor superfamily member 11B
Ligandability
Cysteine 145 of Tumor necrosis factor receptor superfamily member 11B
Cysteine 160 of Tumor necrosis factor receptor superfamily member 11B
3urf Z 86 Z 97
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 11B between cysteines 107 and 118 (86 and 97 respectively in this structure).
Details
Redox score ?
88
PDB code
3urf
Structure name
human rankl/opg complex
Structure deposition date
2011-11-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
O00300
Residue number A
107
Residue number B
118
Peptide name
Tumor necrosis factor receptor superfamily member 11B
Ligandability
Cysteine 107 of Tumor necrosis factor receptor superfamily member 11B
Cysteine 118 of Tumor necrosis factor receptor superfamily member 11B
3urf Z 66 Z 84
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 11B between cysteines 87 and 105 (66 and 84 respectively in this structure).
Details
Redox score ?
87
PDB code
3urf
Structure name
human rankl/opg complex
Structure deposition date
2011-11-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
O00300
Residue number A
87
Residue number B
105
Peptide name
Tumor necrosis factor receptor superfamily member 11B
Ligandability
Cysteine 87 of Tumor necrosis factor receptor superfamily member 11B
Cysteine 105 of Tumor necrosis factor receptor superfamily member 11B
3urf Z 20 Z 33
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 11B between cysteines 41 and 54 (20 and 33 respectively in this structure).
Details
Redox score ?
87
PDB code
3urf
Structure name
human rankl/opg complex
Structure deposition date
2011-11-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
O00300
Residue number A
41
Residue number B
54
Peptide name
Tumor necrosis factor receptor superfamily member 11B
Ligandability
Cysteine 41 of Tumor necrosis factor receptor superfamily member 11B
Cysteine 54 of Tumor necrosis factor receptor superfamily member 11B
3urf Z 23 Z 41
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 11B between cysteines 44 and 62 (23 and 41 respectively in this structure).
Details
Redox score ?
86
PDB code
3urf
Structure name
human rankl/opg complex
Structure deposition date
2011-11-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
O00300
Residue number A
44
Residue number B
62
Peptide name
Tumor necrosis factor receptor superfamily member 11B
Ligandability
Cysteine 44 of Tumor necrosis factor receptor superfamily member 11B
Cysteine 62 of Tumor necrosis factor receptor superfamily member 11B
3urf Z 103 Z 139
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 11B between cysteines 124 and 160 (103 and 139 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
58
PDB code
3urf
Structure name
human rankl/opg complex
Structure deposition date
2011-11-22
Thiol separation (Å)
7
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
O00300
Residue number A
124
Residue number B
160
Peptide name
Tumor necrosis factor receptor superfamily member 11B
Ligandability
Cysteine 124 of Tumor necrosis factor receptor superfamily member 11B
Cysteine 160 of Tumor necrosis factor receptor superfamily member 11B
3urf Z 103 Z 124
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 11B between cysteines 124 and 145 (103 and 124 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
57
PDB code
3urf
Structure name
human rankl/opg complex
Structure deposition date
2011-11-22
Thiol separation (Å)
8
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
O00300
Residue number A
124
Residue number B
145
Peptide name
Tumor necrosis factor receptor superfamily member 11B
Ligandability
Cysteine 124 of Tumor necrosis factor receptor superfamily member 11B
Cysteine 145 of Tumor necrosis factor receptor superfamily member 11B
3urf Z 44 Z 62
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 11B between cysteines 65 and 83 (44 and 62 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
3urf
Structure name
human rankl/opg complex
Structure deposition date
2011-11-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
O00300
Residue number A
65
Residue number B
83
Peptide name
Tumor necrosis factor receptor superfamily member 11B
Ligandability
Cysteine 65 of Tumor necrosis factor receptor superfamily member 11B
Cysteine 83 of Tumor necrosis factor receptor superfamily member 11B
3urf Z 121 Z 139
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 11B between cysteines 142 and 160 (121 and 139 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
3urf
Structure name
human rankl/opg complex
Structure deposition date
2011-11-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
O00300
Residue number A
142
Residue number B
160
Peptide name
Tumor necrosis factor receptor superfamily member 11B
Ligandability
Cysteine 142 of Tumor necrosis factor receptor superfamily member 11B
Cysteine 160 of Tumor necrosis factor receptor superfamily member 11B
3urf Z 66 Z 97
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 11B between cysteines 87 and 118 (66 and 97 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
3urf
Structure name
human rankl/opg complex
Structure deposition date
2011-11-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
O00300
Residue number A
87
Residue number B
118
Peptide name
Tumor necrosis factor receptor superfamily member 11B
Ligandability
Cysteine 87 of Tumor necrosis factor receptor superfamily member 11B
Cysteine 118 of Tumor necrosis factor receptor superfamily member 11B
3urf Z 59 Z 62
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 11B between cysteines 80 and 83 (59 and 62 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
3urf
Structure name
human rankl/opg complex
Structure deposition date
2011-11-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
O00300
Residue number A
80
Residue number B
83
Peptide name
Tumor necrosis factor receptor superfamily member 11B
Ligandability
Cysteine 80 of Tumor necrosis factor receptor superfamily member 11B
Cysteine 83 of Tumor necrosis factor receptor superfamily member 11B
3urf Z 121 Z 124
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 11B between cysteines 142 and 145 (121 and 124 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
3urf
Structure name
human rankl/opg complex
Structure deposition date
2011-11-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
O00300
Residue number A
142
Residue number B
145
Peptide name
Tumor necrosis factor receptor superfamily member 11B
Ligandability
Cysteine 142 of Tumor necrosis factor receptor superfamily member 11B
Cysteine 145 of Tumor necrosis factor receptor superfamily member 11B
3urf Z 23 Z 59
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 11B between cysteines 44 and 80 (23 and 59 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
3urf
Structure name
human rankl/opg complex
Structure deposition date
2011-11-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
O00300
Residue number A
44
Residue number B
80
Peptide name
Tumor necrosis factor receptor superfamily member 11B
Ligandability
Cysteine 44 of Tumor necrosis factor receptor superfamily member 11B
Cysteine 80 of Tumor necrosis factor receptor superfamily member 11B
3urf Z 84 Z 97
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 11B between cysteines 105 and 118 (84 and 97 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
3urf
Structure name
human rankl/opg complex
Structure deposition date
2011-11-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
O00300
Residue number A
105
Residue number B
118
Peptide name
Tumor necrosis factor receptor superfamily member 11B
Ligandability
Cysteine 105 of Tumor necrosis factor receptor superfamily member 11B
Cysteine 118 of Tumor necrosis factor receptor superfamily member 11B
3urf Z 44 Z 76
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 11B between cysteines 65 and 97 (44 and 76 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
3urf
Structure name
human rankl/opg complex
Structure deposition date
2011-11-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
O00300
Residue number A
65
Residue number B
97
Peptide name
Tumor necrosis factor receptor superfamily member 11B
Ligandability
Cysteine 65 of Tumor necrosis factor receptor superfamily member 11B
Cysteine 97 of Tumor necrosis factor receptor superfamily member 11B
4e4d R 20 R 41
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 11B between cysteines 41 and 62 (20 and 41 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
4e4d
Structure name
crystal structure of mouse rankl-opg complex
Structure deposition date
2012-03-12
Thiol separation (Å)
9
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
O08712
Residue number A
41
Residue number B
62
Peptide name
Tumor necrosis factor receptor superfamily member 11B
Ligandability
Cysteine 41 of Tumor necrosis factor receptor superfamily member 11B
Cysteine 62 of Tumor necrosis factor receptor superfamily member 11B
3urf Z 23 Z 44
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 11B between cysteines 44 and 65 (23 and 44 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
3urf
Structure name
human rankl/opg complex
Structure deposition date
2011-11-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
O00300
Residue number A
44
Residue number B
65
Peptide name
Tumor necrosis factor receptor superfamily member 11B
Ligandability
Cysteine 44 of Tumor necrosis factor receptor superfamily member 11B
Cysteine 65 of Tumor necrosis factor receptor superfamily member 11B
3urf Z 66 Z 86
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 11B between cysteines 87 and 107 (66 and 86 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
3urf
Structure name
human rankl/opg complex
Structure deposition date
2011-11-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
O00300
Residue number A
87
Residue number B
107
Peptide name
Tumor necrosis factor receptor superfamily member 11B
Ligandability
Cysteine 87 of Tumor necrosis factor receptor superfamily member 11B
Cysteine 107 of Tumor necrosis factor receptor superfamily member 11B
3urf Z 84 Z 86
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 11B between cysteines 105 and 107 (84 and 86 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
3urf
Structure name
human rankl/opg complex
Structure deposition date
2011-11-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
O00300
Residue number A
105
Residue number B
107
Peptide name
Tumor necrosis factor receptor superfamily member 11B
Ligandability
Cysteine 105 of Tumor necrosis factor receptor superfamily member 11B
Cysteine 107 of Tumor necrosis factor receptor superfamily member 11B
4e4d R 33 R 41
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 11B between cysteines 54 and 62 (33 and 41 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
4e4d
Structure name
crystal structure of mouse rankl-opg complex
Structure deposition date
2012-03-12
Thiol separation (Å)
10
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
O08712
Residue number A
54
Residue number B
62
Peptide name
Tumor necrosis factor receptor superfamily member 11B
Ligandability
Cysteine 54 of Tumor necrosis factor receptor superfamily member 11B
Cysteine 62 of Tumor necrosis factor receptor superfamily member 11B
4e4d R 59 R 76
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 11B between cysteines 80 and 97 (59 and 76 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
4e4d
Structure name
crystal structure of mouse rankl-opg complex
Structure deposition date
2012-03-12
Thiol separation (Å)
10
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
O08712
Residue number A
80
Residue number B
97
Peptide name
Tumor necrosis factor receptor superfamily member 11B
Ligandability
Cysteine 80 of Tumor necrosis factor receptor superfamily member 11B
Cysteine 97 of Tumor necrosis factor receptor superfamily member 11B
3urf Z 20 Z 23
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 11B between cysteines 41 and 44 (20 and 23 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
3urf
Structure name
human rankl/opg complex
Structure deposition date
2011-11-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
O00300
Residue number A
41
Residue number B
44
Peptide name
Tumor necrosis factor receptor superfamily member 11B
Ligandability
Cysteine 41 of Tumor necrosis factor receptor superfamily member 11B
Cysteine 44 of Tumor necrosis factor receptor superfamily member 11B
4e4d R 23 R 33
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 11B between cysteines 44 and 54 (23 and 33 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
4e4d
Structure name
crystal structure of mouse rankl-opg complex
Structure deposition date
2012-03-12
Thiol separation (Å)
10
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
O08712
Residue number A
44
Residue number B
54
Peptide name
Tumor necrosis factor receptor superfamily member 11B
Ligandability
Cysteine 44 of Tumor necrosis factor receptor superfamily member 11B
Cysteine 54 of Tumor necrosis factor receptor superfamily member 11B
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