Tumor necrosis factor receptor superfamily member 14
Intermolecular
Cysteine 75 and cysteine 127
Intramolecular
Cysteine 78 and cysteine 93
Cysteine 96 and cysteine 111
Cysteine 42 and cysteine 53
Cysteine 121 and cysteine 138
Cysteine 121 and cysteine 138
Cysteine 54 and cysteine 67
Cysteine 127 and cysteine 135
Cysteine 99 and cysteine 119
Cysteine 57 and cysteine 75
More...Cysteine 121 and cysteine 135
Cysteine 135 and cysteine 138
Cysteine 127 and cysteine 138
Cysteine 121 and cysteine 127
Cysteine 135 and cysteine 138
Cysteine 127 and cysteine 138
Cysteine 67 and cysteine 179
Cysteine 53 and cysteine 54
Cysteine 42 and cysteine 54
Cysteine 78 and cysteine 111
Cysteine 78 and cysteine 111
Cysteine 53 and cysteine 67
Cysteine 57 and cysteine 93
Cysteine 119 and cysteine 138
Cysteine 78 and cysteine 96
Cysteine 57 and cysteine 78
Cysteine 119 and cysteine 138
Cysteine 119 and cysteine 135
Cysteine 67 and cysteine 75
Cysteine 42 and cysteine 67
Cysteine 99 and cysteine 138
Cysteine 93 and cysteine 96
Cysteine 57 and cysteine 67
Cysteine 99 and cysteine 111
Cysteine 75 and cysteine 78
Cysteine 99 and cysteine 138
Cysteine 99 and cysteine 135
Cysteine 54 and cysteine 57
Cysteine 75 and cysteine 93
Cysteine 99 and cysteine 111
5t2r A 41 B 93
A redox-regulated disulphide may form between two units of Tumor necrosis factor receptor superfamily member 14 at cysteines 75 and 127 (41 and 93 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
5t2r
Structure name
unliganded human hvem at 2
Structure deposition date
2016-08-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide A name
Tumor necrosis factor receptor superfamily member 14
Peptide B name
Tumor necrosis factor receptor superfamily member 14
Peptide A accession
Q92956
Peptide B accession
Q92956
Peptide A residue number
75
Peptide B residue number
127
Ligandability
Cysteine 75 of Tumor necrosis factor receptor superfamily member 14
Cysteine 127 of Tumor necrosis factor receptor superfamily member 14
4fhq A 40 A 55
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 14 between cysteines 78 and 93 (40 and 55 respectively in this structure).
Details
Redox score ?
90
PDB code
4fhq
Structure name
crystal structure of hvem
Structure deposition date
2012-06-06
Thiol separation (Å)
2
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q92956
Residue number A
78
Residue number B
93
Peptide name
Tumor necrosis factor receptor superfamily member 14
Ligandability
Cysteine 78 of Tumor necrosis factor receptor superfamily member 14
Cysteine 93 of Tumor necrosis factor receptor superfamily member 14
2aw2 B 58 B 73
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 14 between cysteines 96 and 111 (58 and 73 respectively in this structure).
Details
Redox score ?
89
PDB code
2aw2
Structure name
crystal structure of the human btla-hvem complex
Structure deposition date
2005-08-31
Thiol separation (Å)
2
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q92956
Residue number A
96
Residue number B
111
Peptide name
Tumor necrosis factor receptor superfamily member 14
Ligandability
Cysteine 96 of Tumor necrosis factor receptor superfamily member 14
Cysteine 111 of Tumor necrosis factor receptor superfamily member 14
7msg D 1042 D 1053
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 14 between cysteines 42 and 53 (1042 and 1053 respectively in this structure).
Details
Redox score ?
87
PDB code
7msg
Structure name
the crystal structure of light in complex with hvem and cd160
Structure deposition date
2021-05-11
Thiol separation (Å)
2
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q92956
Residue number A
42
Residue number B
53
Peptide name
Tumor necrosis factor receptor superfamily member 14
Ligandability
Cysteine 42 of Tumor necrosis factor receptor superfamily member 14
Cysteine 53 of Tumor necrosis factor receptor superfamily member 14
7msj A 121 A 138
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 14 between cysteines 121 and 138.
Details
Redox score ?
86
PDB code
7msj
Structure name
the crystal structure of mouse hvem
Structure deposition date
2021-05-11
Thiol separation (Å)
2
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q80WM9
Residue number A
121
Residue number B
138
Peptide name
Tumor necrosis factor receptor superfamily member 14
Ligandability
Cysteine 121 of Tumor necrosis factor receptor superfamily member 14
Cysteine 138 of Tumor necrosis factor receptor superfamily member 14
5t2q A 87 A 104
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 14 between cysteines 121 and 138 (87 and 104 respectively in this structure).
Details
Redox score ?
86
PDB code
5t2q
Structure name
unliganded human hvem at 1
Structure deposition date
2016-08-24
Thiol separation (Å)
2
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q92956
Residue number A
121
Residue number B
138
Peptide name
Tumor necrosis factor receptor superfamily member 14
Ligandability
Cysteine 121 of Tumor necrosis factor receptor superfamily member 14
Cysteine 138 of Tumor necrosis factor receptor superfamily member 14
4rsu E 54 E 67
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 14 between cysteines 54 and 67.
Details
Redox score ?
85
PDB code
4rsu
Structure name
crystal structure of the light and hvem complex
Structure deposition date
2014-11-11
Thiol separation (Å)
2
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q92956
Residue number A
54
Residue number B
67
Peptide name
Tumor necrosis factor receptor superfamily member 14
Ligandability
Cysteine 54 of Tumor necrosis factor receptor superfamily member 14
Cysteine 67 of Tumor necrosis factor receptor superfamily member 14
7msg D 1127 D 1135
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 14 between cysteines 127 and 135 (1127 and 1135 respectively in this structure).
Details
Redox score ?
85
PDB code
7msg
Structure name
the crystal structure of light in complex with hvem and cd160
Structure deposition date
2021-05-11
Thiol separation (Å)
2
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q92956
Residue number A
127
Residue number B
135
Peptide name
Tumor necrosis factor receptor superfamily member 14
Ligandability
Cysteine 127 of Tumor necrosis factor receptor superfamily member 14
Cysteine 135 of Tumor necrosis factor receptor superfamily member 14
7msg E 1099 E 1119
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 14 between cysteines 99 and 119 (1099 and 1119 respectively in this structure).
Details
Redox score ?
84
PDB code
7msg
Structure name
the crystal structure of light in complex with hvem and cd160
Structure deposition date
2021-05-11
Thiol separation (Å)
2
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q92956
Residue number A
99
Residue number B
119
Peptide name
Tumor necrosis factor receptor superfamily member 14
Ligandability
Cysteine 99 of Tumor necrosis factor receptor superfamily member 14
Cysteine 119 of Tumor necrosis factor receptor superfamily member 14
7msg F 1057 F 1075
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 14 between cysteines 57 and 75 (1057 and 1075 respectively in this structure).
Details
Redox score ?
82
PDB code
7msg
Structure name
the crystal structure of light in complex with hvem and cd160
Structure deposition date
2021-05-11
Thiol separation (Å)
2
Half-sphere exposure sum ?
90
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q92956
Residue number A
57
Residue number B
75
Peptide name
Tumor necrosis factor receptor superfamily member 14
Ligandability
Cysteine 57 of Tumor necrosis factor receptor superfamily member 14
Cysteine 75 of Tumor necrosis factor receptor superfamily member 14
7msg D 1121 D 1135
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 14 between cysteines 121 and 135 (1121 and 1135 respectively in this structure).
Details
Redox score ?
77
PDB code
7msg
Structure name
the crystal structure of light in complex with hvem and cd160
Structure deposition date
2021-05-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q92956
Residue number A
121
Residue number B
135
Peptide name
Tumor necrosis factor receptor superfamily member 14
Ligandability
Cysteine 121 of Tumor necrosis factor receptor superfamily member 14
Cysteine 135 of Tumor necrosis factor receptor superfamily member 14
4fhq A 97 A 100
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 14 between cysteines 135 and 138 (97 and 100 respectively in this structure).
Details
Redox score ?
74
PDB code
4fhq
Structure name
crystal structure of hvem
Structure deposition date
2012-06-06
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q92956
Residue number A
135
Residue number B
138
Peptide name
Tumor necrosis factor receptor superfamily member 14
Ligandability
Cysteine 135 of Tumor necrosis factor receptor superfamily member 14
Cysteine 138 of Tumor necrosis factor receptor superfamily member 14
4fhq A 89 A 100
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 14 between cysteines 127 and 138 (89 and 100 respectively in this structure).
Details
Redox score ?
69
PDB code
4fhq
Structure name
crystal structure of hvem
Structure deposition date
2012-06-06
Thiol separation (Å)
6
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q92956
Residue number A
127
Residue number B
138
Peptide name
Tumor necrosis factor receptor superfamily member 14
Ligandability
Cysteine 127 of Tumor necrosis factor receptor superfamily member 14
Cysteine 138 of Tumor necrosis factor receptor superfamily member 14
4rsu F 121 F 127
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 14 between cysteines 121 and 127.
Details
Redox score ?
65
PDB code
4rsu
Structure name
crystal structure of the light and hvem complex
Structure deposition date
2014-11-11
Thiol separation (Å)
5
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q92956
Residue number A
121
Residue number B
127
Peptide name
Tumor necrosis factor receptor superfamily member 14
Ligandability
Cysteine 121 of Tumor necrosis factor receptor superfamily member 14
Cysteine 127 of Tumor necrosis factor receptor superfamily member 14
7msj A 135 A 138
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 14 between cysteines 135 and 138.
Details
Redox score ?
65
PDB code
7msj
Structure name
the crystal structure of mouse hvem
Structure deposition date
2021-05-11
Thiol separation (Å)
6
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q80WM9
Residue number A
135
Residue number B
138
Peptide name
Tumor necrosis factor receptor superfamily member 14
Ligandability
Cysteine 135 of Tumor necrosis factor receptor superfamily member 14
Cysteine 138 of Tumor necrosis factor receptor superfamily member 14
7msj A 127 A 138
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 14 between cysteines 127 and 138.
Details
Redox score ?
64
PDB code
7msj
Structure name
the crystal structure of mouse hvem
Structure deposition date
2021-05-11
Thiol separation (Å)
6
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q80WM9
Residue number A
127
Residue number B
138
Peptide name
Tumor necrosis factor receptor superfamily member 14
Ligandability
Cysteine 127 of Tumor necrosis factor receptor superfamily member 14
Cysteine 138 of Tumor necrosis factor receptor superfamily member 14
6ng3 A 61 A 113
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 14 between cysteines 67 and 179 (61 and 113 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
55
PDB code
6ng3
Structure name
crystal structure of human cd160 and hvem complex
Structure deposition date
2018-12-21
Thiol separation (Å)
5
Half-sphere exposure sum ?
88
Minimum pKa ?
11
% buried
nan
Peptide accession
Q92956
Residue number A
67
Residue number B
179
Peptide name
Tumor necrosis factor receptor superfamily member 14
Ligandability
Cysteine 67 of Tumor necrosis factor receptor superfamily member 14
Cysteine 179 of Tumor necrosis factor receptor superfamily member 14
4rsu D 53 D 54
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 14 between cysteines 53 and 54. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
4rsu
Structure name
crystal structure of the light and hvem complex
Structure deposition date
2014-11-11
Thiol separation (Å)
8
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q92956
Residue number A
53
Residue number B
54
Peptide name
Tumor necrosis factor receptor superfamily member 14
Ligandability
Cysteine 53 of Tumor necrosis factor receptor superfamily member 14
Cysteine 54 of Tumor necrosis factor receptor superfamily member 14
4rsu J 42 J 54
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 14 between cysteines 42 and 54. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
4rsu
Structure name
crystal structure of the light and hvem complex
Structure deposition date
2014-11-11
Thiol separation (Å)
8
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q92956
Residue number A
42
Residue number B
54
Peptide name
Tumor necrosis factor receptor superfamily member 14
Ligandability
Cysteine 42 of Tumor necrosis factor receptor superfamily member 14
Cysteine 54 of Tumor necrosis factor receptor superfamily member 14
7msg E 1078 E 1111
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 14 between cysteines 78 and 111 (1078 and 1111 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
7msg
Structure name
the crystal structure of light in complex with hvem and cd160
Structure deposition date
2021-05-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q92956
Residue number A
78
Residue number B
111
Peptide name
Tumor necrosis factor receptor superfamily member 14
Ligandability
Cysteine 78 of Tumor necrosis factor receptor superfamily member 14
Cysteine 111 of Tumor necrosis factor receptor superfamily member 14
7msj A 78 A 111
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 14 between cysteines 78 and 111. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
7msj
Structure name
the crystal structure of mouse hvem
Structure deposition date
2021-05-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q80WM9
Residue number A
78
Residue number B
111
Peptide name
Tumor necrosis factor receptor superfamily member 14
Ligandability
Cysteine 78 of Tumor necrosis factor receptor superfamily member 14
Cysteine 111 of Tumor necrosis factor receptor superfamily member 14
4rsu D 53 D 67
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 14 between cysteines 53 and 67. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
4rsu
Structure name
crystal structure of the light and hvem complex
Structure deposition date
2014-11-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q92956
Residue number A
53
Residue number B
67
Peptide name
Tumor necrosis factor receptor superfamily member 14
Ligandability
Cysteine 53 of Tumor necrosis factor receptor superfamily member 14
Cysteine 67 of Tumor necrosis factor receptor superfamily member 14
5t2q A 23 A 59
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 14 between cysteines 57 and 93 (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 ?
48
PDB code
5t2q
Structure name
unliganded human hvem at 1
Structure deposition date
2016-08-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q92956
Residue number A
57
Residue number B
93
Peptide name
Tumor necrosis factor receptor superfamily member 14
Ligandability
Cysteine 57 of Tumor necrosis factor receptor superfamily member 14
Cysteine 93 of Tumor necrosis factor receptor superfamily member 14
1jma B 81 B 100
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 14 between cysteines 119 and 138 (81 and 100 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
1jma
Structure name
crystal structure of the herpes simplex virus glycoprotein d bound to the cellular receptor hvea/hvem
Structure deposition date
2001-07-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q92956
Residue number A
119
Residue number B
138
Peptide name
Tumor necrosis factor receptor superfamily member 14
Ligandability
Cysteine 119 of Tumor necrosis factor receptor superfamily member 14
Cysteine 138 of Tumor necrosis factor receptor superfamily member 14
4rsu K 78 K 96
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 14 between cysteines 78 and 96. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
4rsu
Structure name
crystal structure of the light and hvem complex
Structure deposition date
2014-11-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q92956
Residue number A
78
Residue number B
96
Peptide name
Tumor necrosis factor receptor superfamily member 14
Ligandability
Cysteine 78 of Tumor necrosis factor receptor superfamily member 14
Cysteine 96 of Tumor necrosis factor receptor superfamily member 14
5t2r B 23 B 44
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 14 between cysteines 57 and 78 (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 ?
48
PDB code
5t2r
Structure name
unliganded human hvem at 2
Structure deposition date
2016-08-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q92956
Residue number A
57
Residue number B
78
Peptide name
Tumor necrosis factor receptor superfamily member 14
Ligandability
Cysteine 57 of Tumor necrosis factor receptor superfamily member 14
Cysteine 78 of Tumor necrosis factor receptor superfamily member 14
7msj A 119 A 138
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 14 between cysteines 119 and 138. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
7msj
Structure name
the crystal structure of mouse hvem
Structure deposition date
2021-05-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q80WM9
Residue number A
119
Residue number B
138
Peptide name
Tumor necrosis factor receptor superfamily member 14
Ligandability
Cysteine 119 of Tumor necrosis factor receptor superfamily member 14
Cysteine 138 of Tumor necrosis factor receptor superfamily member 14
5t2r A 85 A 101
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 14 between cysteines 119 and 135 (85 and 101 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
5t2r
Structure name
unliganded human hvem at 2
Structure deposition date
2016-08-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q92956
Residue number A
119
Residue number B
135
Peptide name
Tumor necrosis factor receptor superfamily member 14
Ligandability
Cysteine 119 of Tumor necrosis factor receptor superfamily member 14
Cysteine 135 of Tumor necrosis factor receptor superfamily member 14
2aw2 B 29 B 37
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 14 between cysteines 67 and 75 (29 and 37 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
2aw2
Structure name
crystal structure of the human btla-hvem complex
Structure deposition date
2005-08-31
Thiol separation (Å)
9
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q92956
Residue number A
67
Residue number B
75
Peptide name
Tumor necrosis factor receptor superfamily member 14
Ligandability
Cysteine 67 of Tumor necrosis factor receptor superfamily member 14
Cysteine 75 of Tumor necrosis factor receptor superfamily member 14
2aw2 Y 4 Y 29
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 14 between cysteines 42 and 67 (4 and 29 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
2aw2
Structure name
crystal structure of the human btla-hvem complex
Structure deposition date
2005-08-31
Thiol separation (Å)
10
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q92956
Residue number A
42
Residue number B
67
Peptide name
Tumor necrosis factor receptor superfamily member 14
Ligandability
Cysteine 42 of Tumor necrosis factor receptor superfamily member 14
Cysteine 67 of Tumor necrosis factor receptor superfamily member 14
7msj A 99 A 138
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 14 between cysteines 99 and 138. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
7msj
Structure name
the crystal structure of mouse hvem
Structure deposition date
2021-05-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q80WM9
Residue number A
99
Residue number B
138
Peptide name
Tumor necrosis factor receptor superfamily member 14
Ligandability
Cysteine 99 of Tumor necrosis factor receptor superfamily member 14
Cysteine 138 of Tumor necrosis factor receptor superfamily member 14
7msg D 1093 D 1096
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 14 between cysteines 93 and 96 (1093 and 1096 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
7msg
Structure name
the crystal structure of light in complex with hvem and cd160
Structure deposition date
2021-05-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q92956
Residue number A
93
Residue number B
96
Peptide name
Tumor necrosis factor receptor superfamily member 14
Ligandability
Cysteine 93 of Tumor necrosis factor receptor superfamily member 14
Cysteine 96 of Tumor necrosis factor receptor superfamily member 14
2aw2 B 19 B 29
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 14 between cysteines 57 and 67 (19 and 29 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
2aw2
Structure name
crystal structure of the human btla-hvem complex
Structure deposition date
2005-08-31
Thiol separation (Å)
9
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q92956
Residue number A
57
Residue number B
67
Peptide name
Tumor necrosis factor receptor superfamily member 14
Ligandability
Cysteine 57 of Tumor necrosis factor receptor superfamily member 14
Cysteine 67 of Tumor necrosis factor receptor superfamily member 14
7msj A 99 A 111
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 14 between cysteines 99 and 111. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
7msj
Structure name
the crystal structure of mouse hvem
Structure deposition date
2021-05-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q80WM9
Residue number A
99
Residue number B
111
Peptide name
Tumor necrosis factor receptor superfamily member 14
Ligandability
Cysteine 99 of Tumor necrosis factor receptor superfamily member 14
Cysteine 111 of Tumor necrosis factor receptor superfamily member 14
5t2r B 41 B 44
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 14 between cysteines 75 and 78 (41 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 ?
43
PDB code
5t2r
Structure name
unliganded human hvem at 2
Structure deposition date
2016-08-24
Thiol separation (Å)
10
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q92956
Residue number A
75
Residue number B
78
Peptide name
Tumor necrosis factor receptor superfamily member 14
Ligandability
Cysteine 75 of Tumor necrosis factor receptor superfamily member 14
Cysteine 78 of Tumor necrosis factor receptor superfamily member 14
5t2q B 65 B 104
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 14 between cysteines 99 and 138 (65 and 104 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
5t2q
Structure name
unliganded human hvem at 1
Structure deposition date
2016-08-24
Thiol separation (Å)
10
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q92956
Residue number A
99
Residue number B
138
Peptide name
Tumor necrosis factor receptor superfamily member 14
Ligandability
Cysteine 99 of Tumor necrosis factor receptor superfamily member 14
Cysteine 138 of Tumor necrosis factor receptor superfamily member 14
4fhq A 61 A 97
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 14 between cysteines 99 and 135 (61 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 ?
43
PDB code
4fhq
Structure name
crystal structure of hvem
Structure deposition date
2012-06-06
Thiol separation (Å)
10
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q92956
Residue number A
99
Residue number B
135
Peptide name
Tumor necrosis factor receptor superfamily member 14
Ligandability
Cysteine 99 of Tumor necrosis factor receptor superfamily member 14
Cysteine 135 of Tumor necrosis factor receptor superfamily member 14
4rsu F 54 F 57
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 14 between cysteines 54 and 57. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
4rsu
Structure name
crystal structure of the light and hvem complex
Structure deposition date
2014-11-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q92956
Residue number A
54
Residue number B
57
Peptide name
Tumor necrosis factor receptor superfamily member 14
Ligandability
Cysteine 54 of Tumor necrosis factor receptor superfamily member 14
Cysteine 57 of Tumor necrosis factor receptor superfamily member 14
5t2r A 41 A 59
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 14 between cysteines 75 and 93 (41 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 ?
42
PDB code
5t2r
Structure name
unliganded human hvem at 2
Structure deposition date
2016-08-24
Thiol separation (Å)
10
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q92956
Residue number A
75
Residue number B
93
Peptide name
Tumor necrosis factor receptor superfamily member 14
Ligandability
Cysteine 75 of Tumor necrosis factor receptor superfamily member 14
Cysteine 93 of Tumor necrosis factor receptor superfamily member 14
7msg E 1099 E 1111
A redox-regulated disulphide may form within Tumor necrosis factor receptor superfamily member 14 between cysteines 99 and 111 (1099 and 1111 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
7msg
Structure name
the crystal structure of light in complex with hvem and cd160
Structure deposition date
2021-05-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q92956
Residue number A
99
Residue number B
111
Peptide name
Tumor necrosis factor receptor superfamily member 14
Ligandability
Cysteine 99 of Tumor necrosis factor receptor superfamily member 14
Cysteine 111 of Tumor necrosis factor receptor superfamily member 14
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