Tumor necrosis factor receptor superfamily member 11A
Intramolecular
Cysteine 72 and cysteine 87
Cysteine 155 and cysteine 170
Cysteine 176 and cysteine 195
Cysteine 35 and cysteine 47
Cysteine 48 and cysteine 61
Cysteine 51 and cysteine 69
Cysteine 134 and cysteine 152
Cysteine 93 and cysteine 113
Cysteine 125 and cysteine 127
Cysteine 115 and cysteine 128
More...Cysteine 47 and cysteine 48
Cysteine 127 and cysteine 128
Cysteine 35 and cysteine 48
Cysteine 134 and cysteine 170
Cysteine 125 and cysteine 128
Cysteine 134 and cysteine 155
Cysteine 115 and cysteine 125
Cysteine 115 and cysteine 127
Cysteine 47 and cysteine 61
Cysteine 113 and cysteine 128
Cysteine 51 and cysteine 72
Cysteine 35 and cysteine 61
Cysteine 51 and cysteine 87
Cysteine 152 and cysteine 170
Cysteine 152 and cysteine 155
Cysteine 113 and cysteine 115
Cysteine 61 and cysteine 69
Cysteine 93 and cysteine 128
3me4 B 72 B 87
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 11A between cysteines 72 and 87.
Details
Redox score ?
89
PDB code
3me4
Structure name
crystal structure of mouse rank
Structure deposition date
2010-03-31
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
O35305
Residue number A
72
Residue number B
87
Peptide name
Tumor necrosis factor receptor superfamily member 11A
Ligandability
Cysteine 72 of Tumor necrosis factor receptor superfamily member 11A
Cysteine 87 of Tumor necrosis factor receptor superfamily member 11A
5bnq R 155 R 170
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 11A between cysteines 155 and 170.
Details
Redox score ?
89
PDB code
5bnq
Structure name
crystal structure of hrankl-mrank complex
Structure deposition date
2015-05-26
Thiol separation (Å)
2
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
O35305
Residue number A
155
Residue number B
170
Peptide name
Tumor necrosis factor receptor superfamily member 11A
Ligandability
Cysteine 155 of Tumor necrosis factor receptor superfamily member 11A
Cysteine 170 of Tumor necrosis factor receptor superfamily member 11A
3me4 A 176 A 195
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 11A between cysteines 176 and 195.
Details
Redox score ?
88
PDB code
3me4
Structure name
crystal structure of mouse rank
Structure deposition date
2010-03-31
Thiol separation (Å)
2
Half-sphere exposure sum ?
44
Minimum pKa ?
nan
% buried
nan
Peptide accession
O35305
Residue number A
176
Residue number B
195
Peptide name
Tumor necrosis factor receptor superfamily member 11A
Ligandability
Cysteine 176 of Tumor necrosis factor receptor superfamily member 11A
Cysteine 195 of Tumor necrosis factor receptor superfamily member 11A
3me2 R 35 R 47
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 11A between cysteines 35 and 47.
Details
Redox score ?
87
PDB code
3me2
Structure name
crystal structure of mouse rankl-rank complex
Structure deposition date
2010-03-31
Thiol separation (Å)
2
Half-sphere exposure sum ?
36
Minimum pKa ?
nan
% buried
nan
Peptide accession
O35305
Residue number A
35
Residue number B
47
Peptide name
Tumor necrosis factor receptor superfamily member 11A
Ligandability
Cysteine 35 of Tumor necrosis factor receptor superfamily member 11A
Cysteine 47 of Tumor necrosis factor receptor superfamily member 11A
4giq R 18 R 31
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 11A between cysteines 48 and 61 (18 and 31 respectively in this structure).
Details
Redox score ?
87
PDB code
4giq
Structure name
crystal structure of mouse rank bound to rankl
Structure deposition date
2012-08-08
Thiol separation (Å)
2
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
O35305
Residue number A
48
Residue number B
61
Peptide name
Tumor necrosis factor receptor superfamily member 11A
Ligandability
Cysteine 48 of Tumor necrosis factor receptor superfamily member 11A
Cysteine 61 of Tumor necrosis factor receptor superfamily member 11A
4giq R 21 R 39
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 11A between cysteines 51 and 69 (21 and 39 respectively in this structure).
Details
Redox score ?
86
PDB code
4giq
Structure name
crystal structure of mouse rank bound to rankl
Structure deposition date
2012-08-08
Thiol separation (Å)
2
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
O35305
Residue number A
51
Residue number B
69
Peptide name
Tumor necrosis factor receptor superfamily member 11A
Ligandability
Cysteine 51 of Tumor necrosis factor receptor superfamily member 11A
Cysteine 69 of Tumor necrosis factor receptor superfamily member 11A
4giq R 104 R 122
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 11A between cysteines 134 and 152 (104 and 122 respectively in this structure).
Details
Redox score ?
86
PDB code
4giq
Structure name
crystal structure of mouse rank bound to rankl
Structure deposition date
2012-08-08
Thiol separation (Å)
2
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
O35305
Residue number A
134
Residue number B
152
Peptide name
Tumor necrosis factor receptor superfamily member 11A
Ligandability
Cysteine 134 of Tumor necrosis factor receptor superfamily member 11A
Cysteine 152 of Tumor necrosis factor receptor superfamily member 11A
4giq R 63 R 83
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 11A between cysteines 93 and 113 (63 and 83 respectively in this structure).
Details
Redox score ?
86
PDB code
4giq
Structure name
crystal structure of mouse rank bound to rankl
Structure deposition date
2012-08-08
Thiol separation (Å)
2
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
O35305
Residue number A
93
Residue number B
113
Peptide name
Tumor necrosis factor receptor superfamily member 11A
Ligandability
Cysteine 93 of Tumor necrosis factor receptor superfamily member 11A
Cysteine 113 of Tumor necrosis factor receptor superfamily member 11A
3me4 B 125 B 127
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 11A between cysteines 125 and 127.
Details
Redox score ?
85
PDB code
3me4
Structure name
crystal structure of mouse rank
Structure deposition date
2010-03-31
Thiol separation (Å)
2
Half-sphere exposure sum ?
34
Minimum pKa ?
nan
% buried
nan
Peptide accession
O35305
Residue number A
125
Residue number B
127
Peptide name
Tumor necrosis factor receptor superfamily member 11A
Ligandability
Cysteine 125 of Tumor necrosis factor receptor superfamily member 11A
Cysteine 127 of Tumor necrosis factor receptor superfamily member 11A
3me4 A 115 A 128
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 11A between cysteines 115 and 128.
Details
Redox score ?
84
PDB code
3me4
Structure name
crystal structure of mouse rank
Structure deposition date
2010-03-31
Thiol separation (Å)
2
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
O35305
Residue number A
115
Residue number B
128
Peptide name
Tumor necrosis factor receptor superfamily member 11A
Ligandability
Cysteine 115 of Tumor necrosis factor receptor superfamily member 11A
Cysteine 128 of Tumor necrosis factor receptor superfamily member 11A
3me2 R 47 R 48
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 11A between cysteines 47 and 48. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
56
PDB code
3me2
Structure name
crystal structure of mouse rankl-rank complex
Structure deposition date
2010-03-31
Thiol separation (Å)
7
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
O35305
Residue number A
47
Residue number B
48
Peptide name
Tumor necrosis factor receptor superfamily member 11A
Ligandability
Cysteine 47 of Tumor necrosis factor receptor superfamily member 11A
Cysteine 48 of Tumor necrosis factor receptor superfamily member 11A
3qbq D 127 D 128
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 11A between cysteines 127 and 128. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
53
PDB code
3qbq
Structure name
crystal structure of extracellular domains of mouse rank-rankl complex
Structure deposition date
2011-01-13
Thiol separation (Å)
7
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
O35305
Residue number A
127
Residue number B
128
Peptide name
Tumor necrosis factor receptor superfamily member 11A
Ligandability
Cysteine 127 of Tumor necrosis factor receptor superfamily member 11A
Cysteine 128 of Tumor necrosis factor receptor superfamily member 11A
3qbq D 35 D 48
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 11A between cysteines 35 and 48. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
52
PDB code
3qbq
Structure name
crystal structure of extracellular domains of mouse rank-rankl complex
Structure deposition date
2011-01-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
O35305
Residue number A
35
Residue number B
48
Peptide name
Tumor necrosis factor receptor superfamily member 11A
Ligandability
Cysteine 35 of Tumor necrosis factor receptor superfamily member 11A
Cysteine 48 of Tumor necrosis factor receptor superfamily member 11A
3qbq D 134 D 170
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 11A between cysteines 134 and 170. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
3qbq
Structure name
crystal structure of extracellular domains of mouse rank-rankl complex
Structure deposition date
2011-01-13
Thiol separation (Å)
8
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
O35305
Residue number A
134
Residue number B
170
Peptide name
Tumor necrosis factor receptor superfamily member 11A
Ligandability
Cysteine 134 of Tumor necrosis factor receptor superfamily member 11A
Cysteine 170 of Tumor necrosis factor receptor superfamily member 11A
4giq R 95 R 98
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 11A between cysteines 125 and 128 (95 and 98 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
4giq
Structure name
crystal structure of mouse rank bound to rankl
Structure deposition date
2012-08-08
Thiol separation (Å)
8
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
O35305
Residue number A
125
Residue number B
128
Peptide name
Tumor necrosis factor receptor superfamily member 11A
Ligandability
Cysteine 125 of Tumor necrosis factor receptor superfamily member 11A
Cysteine 128 of Tumor necrosis factor receptor superfamily member 11A
5bnq R 134 R 155
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 11A between cysteines 134 and 155. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
5bnq
Structure name
crystal structure of hrankl-mrank complex
Structure deposition date
2015-05-26
Thiol separation (Å)
9
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
O35305
Residue number A
134
Residue number B
155
Peptide name
Tumor necrosis factor receptor superfamily member 11A
Ligandability
Cysteine 134 of Tumor necrosis factor receptor superfamily member 11A
Cysteine 155 of Tumor necrosis factor receptor superfamily member 11A
3me4 A 115 A 125
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 11A between cysteines 115 and 125. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
3me4
Structure name
crystal structure of mouse rank
Structure deposition date
2010-03-31
Thiol separation (Å)
8
Half-sphere exposure sum ?
47
Minimum pKa ?
nan
% buried
nan
Peptide accession
O35305
Residue number A
115
Residue number B
125
Peptide name
Tumor necrosis factor receptor superfamily member 11A
Ligandability
Cysteine 115 of Tumor necrosis factor receptor superfamily member 11A
Cysteine 125 of Tumor necrosis factor receptor superfamily member 11A
3me4 B 115 B 127
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 11A between cysteines 115 and 127. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
3me4
Structure name
crystal structure of mouse rank
Structure deposition date
2010-03-31
Thiol separation (Å)
8
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
O35305
Residue number A
115
Residue number B
127
Peptide name
Tumor necrosis factor receptor superfamily member 11A
Ligandability
Cysteine 115 of Tumor necrosis factor receptor superfamily member 11A
Cysteine 127 of Tumor necrosis factor receptor superfamily member 11A
3me2 R 47 R 61
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 11A between cysteines 47 and 61. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
3me2
Structure name
crystal structure of mouse rankl-rank complex
Structure deposition date
2010-03-31
Thiol separation (Å)
9
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide accession
O35305
Residue number A
47
Residue number B
61
Peptide name
Tumor necrosis factor receptor superfamily member 11A
Ligandability
Cysteine 47 of Tumor necrosis factor receptor superfamily member 11A
Cysteine 61 of Tumor necrosis factor receptor superfamily member 11A
5bnq R 113 R 128
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 11A between cysteines 113 and 128. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
5bnq
Structure name
crystal structure of hrankl-mrank complex
Structure deposition date
2015-05-26
Thiol separation (Å)
9
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
O35305
Residue number A
113
Residue number B
128
Peptide name
Tumor necrosis factor receptor superfamily member 11A
Ligandability
Cysteine 113 of Tumor necrosis factor receptor superfamily member 11A
Cysteine 128 of Tumor necrosis factor receptor superfamily member 11A
3me4 A 51 A 72
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 11A between cysteines 51 and 72. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
3me4
Structure name
crystal structure of mouse rank
Structure deposition date
2010-03-31
Thiol separation (Å)
9
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
O35305
Residue number A
51
Residue number B
72
Peptide name
Tumor necrosis factor receptor superfamily member 11A
Ligandability
Cysteine 51 of Tumor necrosis factor receptor superfamily member 11A
Cysteine 72 of Tumor necrosis factor receptor superfamily member 11A
4giq R 5 R 31
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 11A between cysteines 35 and 61 (5 and 31 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
4giq
Structure name
crystal structure of mouse rank bound to rankl
Structure deposition date
2012-08-08
Thiol separation (Å)
10
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
O35305
Residue number A
35
Residue number B
61
Peptide name
Tumor necrosis factor receptor superfamily member 11A
Ligandability
Cysteine 35 of Tumor necrosis factor receptor superfamily member 11A
Cysteine 61 of Tumor necrosis factor receptor superfamily member 11A
3qbq B 51 B 87
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 11A between cysteines 51 and 87. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
3qbq
Structure name
crystal structure of extracellular domains of mouse rank-rankl complex
Structure deposition date
2011-01-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
O35305
Residue number A
51
Residue number B
87
Peptide name
Tumor necrosis factor receptor superfamily member 11A
Ligandability
Cysteine 51 of Tumor necrosis factor receptor superfamily member 11A
Cysteine 87 of Tumor necrosis factor receptor superfamily member 11A
3qbq B 152 B 170
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 11A between cysteines 152 and 170. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
3qbq
Structure name
crystal structure of extracellular domains of mouse rank-rankl complex
Structure deposition date
2011-01-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
O35305
Residue number A
152
Residue number B
170
Peptide name
Tumor necrosis factor receptor superfamily member 11A
Ligandability
Cysteine 152 of Tumor necrosis factor receptor superfamily member 11A
Cysteine 170 of Tumor necrosis factor receptor superfamily member 11A
3qbq B 152 B 155
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 11A between cysteines 152 and 155. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
3qbq
Structure name
crystal structure of extracellular domains of mouse rank-rankl complex
Structure deposition date
2011-01-13
Thiol separation (Å)
10
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
O35305
Residue number A
152
Residue number B
155
Peptide name
Tumor necrosis factor receptor superfamily member 11A
Ligandability
Cysteine 152 of Tumor necrosis factor receptor superfamily member 11A
Cysteine 155 of Tumor necrosis factor receptor superfamily member 11A
3qbq D 113 D 115
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 11A between cysteines 113 and 115. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
3qbq
Structure name
crystal structure of extracellular domains of mouse rank-rankl complex
Structure deposition date
2011-01-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
O35305
Residue number A
113
Residue number B
115
Peptide name
Tumor necrosis factor receptor superfamily member 11A
Ligandability
Cysteine 113 of Tumor necrosis factor receptor superfamily member 11A
Cysteine 115 of Tumor necrosis factor receptor superfamily member 11A
3qbq B 61 B 69
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 11A between cysteines 61 and 69. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
3qbq
Structure name
crystal structure of extracellular domains of mouse rank-rankl complex
Structure deposition date
2011-01-13
Thiol separation (Å)
10
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
O35305
Residue number A
61
Residue number B
69
Peptide name
Tumor necrosis factor receptor superfamily member 11A
Ligandability
Cysteine 61 of Tumor necrosis factor receptor superfamily member 11A
Cysteine 69 of Tumor necrosis factor receptor superfamily member 11A
3qbq B 93 B 128
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 11A between cysteines 93 and 128. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
3qbq
Structure name
crystal structure of extracellular domains of mouse rank-rankl complex
Structure deposition date
2011-01-13
Thiol separation (Å)
10
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
O35305
Residue number A
93
Residue number B
128
Peptide name
Tumor necrosis factor receptor superfamily member 11A
Ligandability
Cysteine 93 of Tumor necrosis factor receptor superfamily member 11A
Cysteine 128 of Tumor necrosis factor receptor superfamily member 11A
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