ELR1
Intramolecular
Cysteine 78 and cysteine 93
Cysteine 96 and cysteine 111
Cysteine 42 and cysteine 53
Cysteine 121 and cysteine 138
Cysteine 57 and cysteine 75
Cysteine 99 and cysteine 119
Cysteine 54 and cysteine 67
Cysteine 127 and cysteine 135
Cysteine 135 and cysteine 138
Cysteine 121 and cysteine 135
More...Cysteine 127 and cysteine 138
Cysteine 121 and cysteine 127
Cysteine 42 and cysteine 54
Cysteine 78 and cysteine 96
Cysteine 53 and cysteine 54
Cysteine 78 and cysteine 111
Cysteine 53 and cysteine 67
Cysteine 42 and cysteine 67
Cysteine 119 and cysteine 135
Cysteine 57 and cysteine 93
Cysteine 93 and cysteine 96
Cysteine 119 and cysteine 138
Cysteine 99 and cysteine 111
Cysteine 99 and cysteine 138
Cysteine 93 and cysteine 111
Cysteine 99 and cysteine 135
Cysteine 57 and cysteine 78
Cysteine 75 and cysteine 93
Cysteine 96 and cysteine 99
Cysteine 119 and cysteine 127
Cysteine 54 and cysteine 75
Cysteine 119 and cysteine 121
Cysteine 111 and cysteine 119
Cysteine 54 and cysteine 57
3wvt A 78 A 93
A redox-regulated disulphide may form within ELR1 between cysteines 78 and 93.
Details
Redox score ?
90
PDB code
3wvt
Structure name
structural and biochemical study of equine lentivirus receptor 1
Structure deposition date
2014-06-07
Thiol separation (Å)
2
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q4G265
Residue number A
78
Residue number B
93
Peptide name
ELR1
Ligandability
Cysteine 78 of ELR1
Cysteine 93 of ELR1
3wvt A 96 A 111
A redox-regulated disulphide may form within ELR1 between cysteines 96 and 111.
Details
Redox score ?
90
PDB code
3wvt
Structure name
structural and biochemical study of equine lentivirus receptor 1
Structure deposition date
2014-06-07
Thiol separation (Å)
2
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q4G265
Residue number A
96
Residue number B
111
Peptide name
ELR1
Ligandability
Cysteine 96 of ELR1
Cysteine 111 of ELR1
3wvt A 42 A 53
A redox-regulated disulphide may form within ELR1 between cysteines 42 and 53.
Details
Redox score ?
88
PDB code
3wvt
Structure name
structural and biochemical study of equine lentivirus receptor 1
Structure deposition date
2014-06-07
Thiol separation (Å)
2
Half-sphere exposure sum ?
40
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q4G265
Residue number A
42
Residue number B
53
Peptide name
ELR1
Ligandability
Cysteine 42 of ELR1
Cysteine 53 of ELR1
3wvt A 121 A 138
A redox-regulated disulphide may form within ELR1 between cysteines 121 and 138.
Details
Redox score ?
87
PDB code
3wvt
Structure name
structural and biochemical study of equine lentivirus receptor 1
Structure deposition date
2014-06-07
Thiol separation (Å)
2
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q4G265
Residue number A
121
Residue number B
138
Peptide name
ELR1
Ligandability
Cysteine 121 of ELR1
Cysteine 138 of ELR1
3wvt A 57 A 75
A redox-regulated disulphide may form within ELR1 between cysteines 57 and 75.
Details
Redox score ?
86
PDB code
3wvt
Structure name
structural and biochemical study of equine lentivirus receptor 1
Structure deposition date
2014-06-07
Thiol separation (Å)
2
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q4G265
Residue number A
57
Residue number B
75
Peptide name
ELR1
Ligandability
Cysteine 57 of ELR1
Cysteine 75 of ELR1
3wvt A 99 A 119
A redox-regulated disulphide may form within ELR1 between cysteines 99 and 119.
Details
Redox score ?
86
PDB code
3wvt
Structure name
structural and biochemical study of equine lentivirus receptor 1
Structure deposition date
2014-06-07
Thiol separation (Å)
2
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q4G265
Residue number A
99
Residue number B
119
Peptide name
ELR1
Ligandability
Cysteine 99 of ELR1
Cysteine 119 of ELR1
3wvt A 54 A 67
A redox-regulated disulphide may form within ELR1 between cysteines 54 and 67.
Details
Redox score ?
86
PDB code
3wvt
Structure name
structural and biochemical study of equine lentivirus receptor 1
Structure deposition date
2014-06-07
Thiol separation (Å)
2
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q4G265
Residue number A
54
Residue number B
67
Peptide name
ELR1
Ligandability
Cysteine 54 of ELR1
Cysteine 67 of ELR1
3wvt A 127 A 135
A redox-regulated disulphide may form within ELR1 between cysteines 127 and 135.
Details
Redox score ?
86
PDB code
3wvt
Structure name
structural and biochemical study of equine lentivirus receptor 1
Structure deposition date
2014-06-07
Thiol separation (Å)
2
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q4G265
Residue number A
127
Residue number B
135
Peptide name
ELR1
Ligandability
Cysteine 127 of ELR1
Cysteine 135 of ELR1
3wvt A 135 A 138
A redox-regulated disulphide may form within ELR1 between cysteines 135 and 138.
Details
Redox score ?
78
PDB code
3wvt
Structure name
structural and biochemical study of equine lentivirus receptor 1
Structure deposition date
2014-06-07
Thiol separation (Å)
3
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q4G265
Residue number A
135
Residue number B
138
Peptide name
ELR1
Ligandability
Cysteine 135 of ELR1
Cysteine 138 of ELR1
3wvt A 121 A 135
A redox-regulated disulphide may form within ELR1 between cysteines 121 and 135.
Details
Redox score ?
74
PDB code
3wvt
Structure name
structural and biochemical study of equine lentivirus receptor 1
Structure deposition date
2014-06-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q4G265
Residue number A
121
Residue number B
135
Peptide name
ELR1
Ligandability
Cysteine 121 of ELR1
Cysteine 135 of ELR1
3wvt A 127 A 138
A redox-regulated disulphide may form within ELR1 between cysteines 127 and 138.
Details
Redox score ?
71
PDB code
3wvt
Structure name
structural and biochemical study of equine lentivirus receptor 1
Structure deposition date
2014-06-07
Thiol separation (Å)
5
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q4G265
Residue number A
127
Residue number B
138
Peptide name
ELR1
Ligandability
Cysteine 127 of ELR1
Cysteine 138 of ELR1
3wvt A 121 A 127
A redox-regulated disulphide may form within ELR1 between cysteines 121 and 127.
Details
Redox score ?
70
PDB code
3wvt
Structure name
structural and biochemical study of equine lentivirus receptor 1
Structure deposition date
2014-06-07
Thiol separation (Å)
5
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q4G265
Residue number A
121
Residue number B
127
Peptide name
ELR1
Ligandability
Cysteine 121 of ELR1
Cysteine 127 of ELR1
3wvt A 42 A 54
A redox-regulated disulphide may form within ELR1 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 ?
55
PDB code
3wvt
Structure name
structural and biochemical study of equine lentivirus receptor 1
Structure deposition date
2014-06-07
Thiol separation (Å)
8
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q4G265
Residue number A
42
Residue number B
54
Peptide name
ELR1
Ligandability
Cysteine 42 of ELR1
Cysteine 54 of ELR1
3wvt A 78 A 96
A redox-regulated disulphide may form within ELR1 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 ?
53
PDB code
3wvt
Structure name
structural and biochemical study of equine lentivirus receptor 1
Structure deposition date
2014-06-07
Thiol separation (Å)
8
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q4G265
Residue number A
78
Residue number B
96
Peptide name
ELR1
Ligandability
Cysteine 78 of ELR1
Cysteine 96 of ELR1
3wvt A 53 A 54
A redox-regulated disulphide may form within ELR1 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 ?
52
PDB code
3wvt
Structure name
structural and biochemical study of equine lentivirus receptor 1
Structure deposition date
2014-06-07
Thiol separation (Å)
8
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q4G265
Residue number A
53
Residue number B
54
Peptide name
ELR1
Ligandability
Cysteine 53 of ELR1
Cysteine 54 of ELR1
3wvt A 78 A 111
A redox-regulated disulphide may form within ELR1 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 ?
51
PDB code
3wvt
Structure name
structural and biochemical study of equine lentivirus receptor 1
Structure deposition date
2014-06-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q4G265
Residue number A
78
Residue number B
111
Peptide name
ELR1
Ligandability
Cysteine 78 of ELR1
Cysteine 111 of ELR1
3wvt A 53 A 67
A redox-regulated disulphide may form within ELR1 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 ?
50
PDB code
3wvt
Structure name
structural and biochemical study of equine lentivirus receptor 1
Structure deposition date
2014-06-07
Thiol separation (Å)
8
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q4G265
Residue number A
53
Residue number B
67
Peptide name
ELR1
Ligandability
Cysteine 53 of ELR1
Cysteine 67 of ELR1
3wvt A 42 A 67
A redox-regulated disulphide may form within ELR1 between cysteines 42 and 67. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
3wvt
Structure name
structural and biochemical study of equine lentivirus receptor 1
Structure deposition date
2014-06-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
42
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q4G265
Residue number A
42
Residue number B
67
Peptide name
ELR1
Ligandability
Cysteine 42 of ELR1
Cysteine 67 of ELR1
3wvt A 119 A 135
A redox-regulated disulphide may form within ELR1 between cysteines 119 and 135. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
3wvt
Structure name
structural and biochemical study of equine lentivirus receptor 1
Structure deposition date
2014-06-07
Thiol separation (Å)
8
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q4G265
Residue number A
119
Residue number B
135
Peptide name
ELR1
Ligandability
Cysteine 119 of ELR1
Cysteine 135 of ELR1
3wvt A 57 A 93
A redox-regulated disulphide may form within ELR1 between cysteines 57 and 93. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
3wvt
Structure name
structural and biochemical study of equine lentivirus receptor 1
Structure deposition date
2014-06-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q4G265
Residue number A
57
Residue number B
93
Peptide name
ELR1
Ligandability
Cysteine 57 of ELR1
Cysteine 93 of ELR1
3wvt A 93 A 96
A redox-regulated disulphide may form within ELR1 between cysteines 93 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
3wvt
Structure name
structural and biochemical study of equine lentivirus receptor 1
Structure deposition date
2014-06-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q4G265
Residue number A
93
Residue number B
96
Peptide name
ELR1
Ligandability
Cysteine 93 of ELR1
Cysteine 96 of ELR1
3wvt A 119 A 138
A redox-regulated disulphide may form within ELR1 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
3wvt
Structure name
structural and biochemical study of equine lentivirus receptor 1
Structure deposition date
2014-06-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q4G265
Residue number A
119
Residue number B
138
Peptide name
ELR1
Ligandability
Cysteine 119 of ELR1
Cysteine 138 of ELR1
3wvt A 99 A 111
A redox-regulated disulphide may form within ELR1 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 ?
46
PDB code
3wvt
Structure name
structural and biochemical study of equine lentivirus receptor 1
Structure deposition date
2014-06-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q4G265
Residue number A
99
Residue number B
111
Peptide name
ELR1
Ligandability
Cysteine 99 of ELR1
Cysteine 111 of ELR1
3wvt A 99 A 138
A redox-regulated disulphide may form within ELR1 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 ?
46
PDB code
3wvt
Structure name
structural and biochemical study of equine lentivirus receptor 1
Structure deposition date
2014-06-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q4G265
Residue number A
99
Residue number B
138
Peptide name
ELR1
Ligandability
Cysteine 99 of ELR1
Cysteine 138 of ELR1
3wvt A 93 A 111
A redox-regulated disulphide may form within ELR1 between cysteines 93 and 111. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
3wvt
Structure name
structural and biochemical study of equine lentivirus receptor 1
Structure deposition date
2014-06-07
Thiol separation (Å)
10
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q4G265
Residue number A
93
Residue number B
111
Peptide name
ELR1
Ligandability
Cysteine 93 of ELR1
Cysteine 111 of ELR1
3wvt A 99 A 135
A redox-regulated disulphide may form within ELR1 between cysteines 99 and 135. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
3wvt
Structure name
structural and biochemical study of equine lentivirus receptor 1
Structure deposition date
2014-06-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q4G265
Residue number A
99
Residue number B
135
Peptide name
ELR1
Ligandability
Cysteine 99 of ELR1
Cysteine 135 of ELR1
3wvt A 57 A 78
A redox-regulated disulphide may form within ELR1 between cysteines 57 and 78. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
3wvt
Structure name
structural and biochemical study of equine lentivirus receptor 1
Structure deposition date
2014-06-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q4G265
Residue number A
57
Residue number B
78
Peptide name
ELR1
Ligandability
Cysteine 57 of ELR1
Cysteine 78 of ELR1
3wvt A 75 A 93
A redox-regulated disulphide may form within ELR1 between cysteines 75 and 93. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
3wvt
Structure name
structural and biochemical study of equine lentivirus receptor 1
Structure deposition date
2014-06-07
Thiol separation (Å)
10
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q4G265
Residue number A
75
Residue number B
93
Peptide name
ELR1
Ligandability
Cysteine 75 of ELR1
Cysteine 93 of ELR1
3wvt A 96 A 99
A redox-regulated disulphide may form within ELR1 between cysteines 96 and 99. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
3wvt
Structure name
structural and biochemical study of equine lentivirus receptor 1
Structure deposition date
2014-06-07
Thiol separation (Å)
10
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q4G265
Residue number A
96
Residue number B
99
Peptide name
ELR1
Ligandability
Cysteine 96 of ELR1
Cysteine 99 of ELR1
3wvt A 119 A 127
A redox-regulated disulphide may form within ELR1 between cysteines 119 and 127. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
3wvt
Structure name
structural and biochemical study of equine lentivirus receptor 1
Structure deposition date
2014-06-07
Thiol separation (Å)
10
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q4G265
Residue number A
119
Residue number B
127
Peptide name
ELR1
Ligandability
Cysteine 119 of ELR1
Cysteine 127 of ELR1
3wvt A 54 A 75
A redox-regulated disulphide may form within ELR1 between cysteines 54 and 75. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
3wvt
Structure name
structural and biochemical study of equine lentivirus receptor 1
Structure deposition date
2014-06-07
Thiol separation (Å)
10
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q4G265
Residue number A
54
Residue number B
75
Peptide name
ELR1
Ligandability
Cysteine 54 of ELR1
Cysteine 75 of ELR1
3wvt A 119 A 121
A redox-regulated disulphide may form within ELR1 between cysteines 119 and 121. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
3wvt
Structure name
structural and biochemical study of equine lentivirus receptor 1
Structure deposition date
2014-06-07
Thiol separation (Å)
10
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q4G265
Residue number A
119
Residue number B
121
Peptide name
ELR1
Ligandability
Cysteine 119 of ELR1
Cysteine 121 of ELR1
3wvt A 111 A 119
A redox-regulated disulphide may form within ELR1 between cysteines 111 and 119. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
3wvt
Structure name
structural and biochemical study of equine lentivirus receptor 1
Structure deposition date
2014-06-07
Thiol separation (Å)
10
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q4G265
Residue number A
111
Residue number B
119
Peptide name
ELR1
Ligandability
Cysteine 111 of ELR1
Cysteine 119 of ELR1
3wvt A 54 A 57
A redox-regulated disulphide may form within ELR1 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 ?
40
PDB code
3wvt
Structure name
structural and biochemical study of equine lentivirus receptor 1
Structure deposition date
2014-06-07
Thiol separation (Å)
10
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q4G265
Residue number A
54
Residue number B
57
Peptide name
ELR1
Ligandability
Cysteine 54 of ELR1
Cysteine 57 of ELR1
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