Protein XRP2
Intramolecular
Cysteine 70 and cysteine 89
Cysteine 86 and cysteine 89
Cysteine 89 and cysteine 108
Cysteine 67 and cysteine 89
Cysteine 67 and cysteine 70
Cysteine 105 and cysteine 122
Cysteine 236 and cysteine 311
Cysteine 114 and cysteine 131
Cysteine 67 and cysteine 86
Cysteine 105 and cysteine 110
More...Cysteine 89 and cysteine 105
Cysteine 105 and cysteine 108
Cysteine 86 and cysteine 105
Cysteine 89 and cysteine 110
Cysteine 108 and cysteine 110
Cysteine 70 and cysteine 86
Cysteine 130 and cysteine 131
Cysteine 110 and cysteine 122
Cysteine 86 and cysteine 122
Cysteine 130 and cysteine 147
Cysteine 70 and cysteine 108
Cysteine 67 and cysteine 108
Cysteine 67 and cysteine 105
Cysteine 108 and cysteine 122
Cysteine 86 and cysteine 108
Cysteine 86 and cysteine 110
Cysteine 114 and cysteine 130
2bx6 A 70 A 89
A redox-regulated disulphide may form within Protein XRP2 between cysteines 70 and 89.
Details
Redox score ?
82
PDB code
2bx6
Structure name
crystal structure of the human retinitis pigmentosa protein 2 (rp2)
Structure deposition date
2005-07-24
Thiol separation (Å)
5
Half-sphere exposure sum ?
70
Minimum pKa ?
3
% buried
40
Peptide accession
O75695
Residue number A
70
Residue number B
89
Peptide name
Protein XRP2
Ligandability
Cysteine 70 of Protein XRP2
Cysteine 89 of Protein XRP2
3bh6 B 86 B 89
A redox-regulated disulphide may form within Protein XRP2 between cysteines 86 and 89.
Details
Redox score ?
81
PDB code
3bh6
Structure name
crystal structure of the rp2-arl3 complex bound to gppnhp
Structure deposition date
2007-11-28
Thiol separation (Å)
5
Half-sphere exposure sum ?
78
Minimum pKa ?
4
% buried
72
Peptide accession
O75695
Residue number A
86
Residue number B
89
Peptide name
Protein XRP2
Ligandability
Cysteine 86 of Protein XRP2
Cysteine 89 of Protein XRP2
2bx6 A 89 A 108
A redox-regulated disulphide may form within Protein XRP2 between cysteines 89 and 108.
Details
Redox score ?
80
PDB code
2bx6
Structure name
crystal structure of the human retinitis pigmentosa protein 2 (rp2)
Structure deposition date
2005-07-24
Thiol separation (Å)
5
Half-sphere exposure sum ?
77
Minimum pKa ?
3
% buried
74
Peptide accession
O75695
Residue number A
89
Residue number B
108
Peptide name
Protein XRP2
Ligandability
Cysteine 89 of Protein XRP2
Cysteine 108 of Protein XRP2
3bh6 B 67 B 89
A redox-regulated disulphide may form within Protein XRP2 between cysteines 67 and 89.
Details
Redox score ?
76
PDB code
3bh6
Structure name
crystal structure of the rp2-arl3 complex bound to gppnhp
Structure deposition date
2007-11-28
Thiol separation (Å)
6
Half-sphere exposure sum ?
72
Minimum pKa ?
4
% buried
54
Peptide accession
O75695
Residue number A
67
Residue number B
89
Peptide name
Protein XRP2
Ligandability
Cysteine 67 of Protein XRP2
Cysteine 89 of Protein XRP2
3bh7 B 67 B 70
A redox-regulated disulphide may form within Protein XRP2 between cysteines 67 and 70.
Details
Redox score ?
76
PDB code
3bh7
Structure name
crystal structure of the rp2-arl3 complex bound to gdp-alf4
Structure deposition date
2007-11-28
Thiol separation (Å)
5
Half-sphere exposure sum ?
64
Minimum pKa ?
7
% buried
35
Peptide accession
O75695
Residue number A
67
Residue number B
70
Peptide name
Protein XRP2
Ligandability
Cysteine 67 of Protein XRP2
Cysteine 70 of Protein XRP2
3bh6 B 105 B 122
A redox-regulated disulphide may form within Protein XRP2 between cysteines 105 and 122.
Details
Redox score ?
71
PDB code
3bh6
Structure name
crystal structure of the rp2-arl3 complex bound to gppnhp
Structure deposition date
2007-11-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
71
Minimum pKa ?
9
% buried
95
Peptide accession
O75695
Residue number A
105
Residue number B
122
Peptide name
Protein XRP2
Ligandability
Cysteine 105 of Protein XRP2
Cysteine 122 of Protein XRP2
3bh6 B 236 B 311
A redox-regulated disulphide may form within Protein XRP2 between cysteines 236 and 311.
Details
Redox score ?
68
PDB code
3bh6
Structure name
crystal structure of the rp2-arl3 complex bound to gppnhp
Structure deposition date
2007-11-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
89
Minimum pKa ?
9
% buried
92
Peptide accession
O75695
Residue number A
236
Residue number B
311
Peptide name
Protein XRP2
Ligandability
Cysteine 236 of Protein XRP2
Cysteine 311 of Protein XRP2
3bh7 B 114 B 131
A redox-regulated disulphide may form within Protein XRP2 between cysteines 114 and 131.
Details
Redox score ?
67
PDB code
3bh7
Structure name
crystal structure of the rp2-arl3 complex bound to gdp-alf4
Structure deposition date
2007-11-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
91
Minimum pKa ?
8
% buried
100
Peptide accession
O75695
Residue number A
114
Residue number B
131
Peptide name
Protein XRP2
Ligandability
Cysteine 114 of Protein XRP2
Cysteine 131 of Protein XRP2
2bx6 A 67 A 86
A redox-regulated disulphide may form within Protein XRP2 between cysteines 67 and 86.
Details
Redox score ?
67
PDB code
2bx6
Structure name
crystal structure of the human retinitis pigmentosa protein 2 (rp2)
Structure deposition date
2005-07-24
Thiol separation (Å)
5
Half-sphere exposure sum ?
72
Minimum pKa ?
11
% buried
52
Peptide accession
O75695
Residue number A
67
Residue number B
86
Peptide name
Protein XRP2
Ligandability
Cysteine 67 of Protein XRP2
Cysteine 86 of Protein XRP2
3bh7 B 105 B 110
A redox-regulated disulphide may form within Protein XRP2 between cysteines 105 and 110.
Details
Redox score ?
65
PDB code
3bh7
Structure name
crystal structure of the rp2-arl3 complex bound to gdp-alf4
Structure deposition date
2007-11-28
Thiol separation (Å)
8
Half-sphere exposure sum ?
84
Minimum pKa ?
1
% buried
98
Peptide accession
O75695
Residue number A
105
Residue number B
110
Peptide name
Protein XRP2
Ligandability
Cysteine 105 of Protein XRP2
Cysteine 110 of Protein XRP2
3bh6 B 89 B 105
A redox-regulated disulphide may form within Protein XRP2 between cysteines 89 and 105.
Details
Redox score ?
61
PDB code
3bh6
Structure name
crystal structure of the rp2-arl3 complex bound to gppnhp
Structure deposition date
2007-11-28
Thiol separation (Å)
8
Half-sphere exposure sum ?
77
Minimum pKa ?
4
% buried
80
Peptide accession
O75695
Residue number A
89
Residue number B
105
Peptide name
Protein XRP2
Ligandability
Cysteine 89 of Protein XRP2
Cysteine 105 of Protein XRP2
2bx6 A 105 A 108
A redox-regulated disulphide may form within Protein XRP2 between cysteines 105 and 108.
Details
Redox score ?
61
PDB code
2bx6
Structure name
crystal structure of the human retinitis pigmentosa protein 2 (rp2)
Structure deposition date
2005-07-24
Thiol separation (Å)
5
Half-sphere exposure sum ?
77
Minimum pKa ?
12
% buried
84
Peptide accession
O75695
Residue number A
105
Residue number B
108
Peptide name
Protein XRP2
Ligandability
Cysteine 105 of Protein XRP2
Cysteine 108 of Protein XRP2
2bx6 A 86 A 105
A redox-regulated disulphide may form within Protein XRP2 between cysteines 86 and 105.
Details
Redox score ?
61
PDB code
2bx6
Structure name
crystal structure of the human retinitis pigmentosa protein 2 (rp2)
Structure deposition date
2005-07-24
Thiol separation (Å)
5
Half-sphere exposure sum ?
78
Minimum pKa ?
13
% buried
72
Peptide accession
O75695
Residue number A
86
Residue number B
105
Peptide name
Protein XRP2
Ligandability
Cysteine 86 of Protein XRP2
Cysteine 105 of Protein XRP2
3bh6 B 89 B 110
A redox-regulated disulphide may form within Protein XRP2 between cysteines 89 and 110. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
53
PDB code
3bh6
Structure name
crystal structure of the rp2-arl3 complex bound to gppnhp
Structure deposition date
2007-11-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
84
Minimum pKa ?
4
% buried
82
Peptide accession
O75695
Residue number A
89
Residue number B
110
Peptide name
Protein XRP2
Ligandability
Cysteine 89 of Protein XRP2
Cysteine 110 of Protein XRP2
3bh6 B 108 B 110
A redox-regulated disulphide may form within Protein XRP2 between cysteines 108 and 110. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
3bh6
Structure name
crystal structure of the rp2-arl3 complex bound to gppnhp
Structure deposition date
2007-11-28
Thiol separation (Å)
6
Half-sphere exposure sum ?
83
Minimum pKa ?
13
% buried
99
Peptide accession
O75695
Residue number A
108
Residue number B
110
Peptide name
Protein XRP2
Ligandability
Cysteine 108 of Protein XRP2
Cysteine 110 of Protein XRP2
3bh6 B 70 B 86
A redox-regulated disulphide may form within Protein XRP2 between cysteines 70 and 86. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
3bh6
Structure name
crystal structure of the rp2-arl3 complex bound to gppnhp
Structure deposition date
2007-11-28
Thiol separation (Å)
8
Half-sphere exposure sum ?
70
Minimum pKa ?
11
% buried
54
Peptide accession
O75695
Residue number A
70
Residue number B
86
Peptide name
Protein XRP2
Ligandability
Cysteine 70 of Protein XRP2
Cysteine 86 of Protein XRP2
3bh6 B 130 B 131
A redox-regulated disulphide may form within Protein XRP2 between cysteines 130 and 131. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
3bh6
Structure name
crystal structure of the rp2-arl3 complex bound to gppnhp
Structure deposition date
2007-11-28
Thiol separation (Å)
8
Half-sphere exposure sum ?
94
Minimum pKa ?
8
% buried
100
Peptide accession
O75695
Residue number A
130
Residue number B
131
Peptide name
Protein XRP2
Ligandability
Cysteine 130 of Protein XRP2
Cysteine 131 of Protein XRP2
2bx6 A 110 A 122
A redox-regulated disulphide may form within Protein XRP2 between cysteines 110 and 122. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
2bx6
Structure name
crystal structure of the human retinitis pigmentosa protein 2 (rp2)
Structure deposition date
2005-07-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
79
Minimum pKa ?
7
% buried
86
Peptide accession
O75695
Residue number A
110
Residue number B
122
Peptide name
Protein XRP2
Ligandability
Cysteine 110 of Protein XRP2
Cysteine 122 of Protein XRP2
3bh6 B 86 B 122
A redox-regulated disulphide may form within Protein XRP2 between cysteines 86 and 122. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
3bh6
Structure name
crystal structure of the rp2-arl3 complex bound to gppnhp
Structure deposition date
2007-11-28
Thiol separation (Å)
10
Half-sphere exposure sum ?
72
Minimum pKa ?
9
% buried
86
Peptide accession
O75695
Residue number A
86
Residue number B
122
Peptide name
Protein XRP2
Ligandability
Cysteine 86 of Protein XRP2
Cysteine 122 of Protein XRP2
3bh6 B 130 B 147
A redox-regulated disulphide may form within Protein XRP2 between cysteines 130 and 147. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
3bh6
Structure name
crystal structure of the rp2-arl3 complex bound to gppnhp
Structure deposition date
2007-11-28
Thiol separation (Å)
7
Half-sphere exposure sum ?
93
Minimum pKa ?
11
% buried
100
Peptide accession
O75695
Residue number A
130
Residue number B
147
Peptide name
Protein XRP2
Ligandability
Cysteine 130 of Protein XRP2
Cysteine 147 of Protein XRP2
2bx6 A 70 A 108
A redox-regulated disulphide may form within Protein XRP2 between cysteines 70 and 108. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
2bx6
Structure name
crystal structure of the human retinitis pigmentosa protein 2 (rp2)
Structure deposition date
2005-07-24
Thiol separation (Å)
10
Half-sphere exposure sum ?
69
Minimum pKa ?
10
% buried
56
Peptide accession
O75695
Residue number A
70
Residue number B
108
Peptide name
Protein XRP2
Ligandability
Cysteine 70 of Protein XRP2
Cysteine 108 of Protein XRP2
2bx6 A 67 A 108
A redox-regulated disulphide may form within Protein XRP2 between cysteines 67 and 108. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
2bx6
Structure name
crystal structure of the human retinitis pigmentosa protein 2 (rp2)
Structure deposition date
2005-07-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
11
% buried
62
Peptide accession
O75695
Residue number A
67
Residue number B
108
Peptide name
Protein XRP2
Ligandability
Cysteine 67 of Protein XRP2
Cysteine 108 of Protein XRP2
3bh6 B 67 B 105
A redox-regulated disulphide may form within Protein XRP2 between cysteines 67 and 105. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
3bh6
Structure name
crystal structure of the rp2-arl3 complex bound to gppnhp
Structure deposition date
2007-11-28
Thiol separation (Å)
10
Half-sphere exposure sum ?
71
Minimum pKa ?
10
% buried
68
Peptide accession
O75695
Residue number A
67
Residue number B
105
Peptide name
Protein XRP2
Ligandability
Cysteine 67 of Protein XRP2
Cysteine 105 of Protein XRP2
3bh7 B 108 B 122
A redox-regulated disulphide may form within Protein XRP2 between cysteines 108 and 122. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
35
PDB code
3bh7
Structure name
crystal structure of the rp2-arl3 complex bound to gdp-alf4
Structure deposition date
2007-11-28
Thiol separation (Å)
8
Half-sphere exposure sum ?
70
Minimum pKa ?
17
% buried
95
Peptide accession
O75695
Residue number A
108
Residue number B
122
Peptide name
Protein XRP2
Ligandability
Cysteine 108 of Protein XRP2
Cysteine 122 of Protein XRP2
3bh7 B 86 B 108
A redox-regulated disulphide may form within Protein XRP2 between cysteines 86 and 108. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
3bh7
Structure name
crystal structure of the rp2-arl3 complex bound to gdp-alf4
Structure deposition date
2007-11-28
Thiol separation (Å)
6
Half-sphere exposure sum ?
76
Minimum pKa ?
22
% buried
86
Peptide accession
O75695
Residue number A
86
Residue number B
108
Peptide name
Protein XRP2
Ligandability
Cysteine 86 of Protein XRP2
Cysteine 108 of Protein XRP2
3bh7 B 86 B 110
A redox-regulated disulphide may form within Protein XRP2 between cysteines 86 and 110. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
31
PDB code
3bh7
Structure name
crystal structure of the rp2-arl3 complex bound to gdp-alf4
Structure deposition date
2007-11-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
85
Minimum pKa ?
13
% buried
89
Peptide accession
O75695
Residue number A
86
Residue number B
110
Peptide name
Protein XRP2
Ligandability
Cysteine 86 of Protein XRP2
Cysteine 110 of Protein XRP2
3bh6 B 114 B 130
A redox-regulated disulphide may form within Protein XRP2 between cysteines 114 and 130. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
31
PDB code
3bh6
Structure name
crystal structure of the rp2-arl3 complex bound to gppnhp
Structure deposition date
2007-11-28
Thiol separation (Å)
8
Half-sphere exposure sum ?
98
Minimum pKa ?
14
% buried
100
Peptide accession
O75695
Residue number A
114
Residue number B
130
Peptide name
Protein XRP2
Ligandability
Cysteine 114 of Protein XRP2
Cysteine 130 of Protein XRP2
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