Adhesion G protein-coupled receptor E2
Intramolecular
Cysteine 47 and cysteine 65
Cysteine 29 and cysteine 39
Cysteine 71 and cysteine 85
Cysteine 96 and cysteine 117
Cysteine 33 and cysteine 45
Cysteine 79 and cysteine 94
Cysteine 223 and cysteine 238
Cysteine 216 and cysteine 229
Cysteine 240 and cysteine 259
Cysteine 223 and cysteine 229
More...Cysteine 79 and cysteine 85
Cysteine 33 and cysteine 39
Cysteine 85 and cysteine 94
Cysteine 216 and cysteine 223
Cysteine 29 and cysteine 33
Cysteine 71 and cysteine 79
Cysteine 229 and cysteine 238
Cysteine 71 and cysteine 94
Cysteine 39 and cysteine 45
Cysteine 29 and cysteine 45
Cysteine 216 and cysteine 238
Cysteine 45 and cysteine 65
Cysteine 79 and cysteine 117
Cysteine 94 and cysteine 117
Cysteine 33 and cysteine 65
Cysteine 238 and cysteine 259
Cysteine 223 and cysteine 259
Cysteine 45 and cysteine 47
Cysteine 238 and cysteine 240
Cysteine 79 and cysteine 96
Cysteine 94 and cysteine 96
Cysteine 33 and cysteine 47
2box A 23 A 41
A redox-regulated disulphide may form within Adhesion G protein-coupled receptor E2 between cysteines 47 and 65 (23 and 41 respectively in this structure).
Details
Redox score ?
87
PDB code
2box
Structure name
egf domains 1,2,5 of human emr2, a 7-tm immune system molecule, in complex with strontium
Structure deposition date
2005-04-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UHX3
Residue number A
47
Residue number B
65
Peptide name
Adhesion G protein-coupled receptor E2
Ligandability
Cysteine 47 of Adhesion G protein-coupled receptor E2
Cysteine 65 of Adhesion G protein-coupled receptor E2
2bou A 5 A 15
A redox-regulated disulphide may form within Adhesion G protein-coupled receptor E2 between cysteines 29 and 39 (5 and 15 respectively in this structure).
Details
Redox score ?
87
PDB code
2bou
Structure name
egf domains 1,2,5 of human emr2, a 7-tm immune system molecule, in complex with barium
Structure deposition date
2005-04-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
42
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UHX3
Residue number A
29
Residue number B
39
Peptide name
Adhesion G protein-coupled receptor E2
Ligandability
Cysteine 29 of Adhesion G protein-coupled receptor E2
Cysteine 39 of Adhesion G protein-coupled receptor E2
2box A 47 A 61
A redox-regulated disulphide may form within Adhesion G protein-coupled receptor E2 between cysteines 71 and 85 (47 and 61 respectively in this structure).
Details
Redox score ?
87
PDB code
2box
Structure name
egf domains 1,2,5 of human emr2, a 7-tm immune system molecule, in complex with strontium
Structure deposition date
2005-04-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UHX3
Residue number A
71
Residue number B
85
Peptide name
Adhesion G protein-coupled receptor E2
Ligandability
Cysteine 71 of Adhesion G protein-coupled receptor E2
Cysteine 85 of Adhesion G protein-coupled receptor E2
2box A 72 A 93
A redox-regulated disulphide may form within Adhesion G protein-coupled receptor E2 between cysteines 96 and 117 (72 and 93 respectively in this structure).
Details
Redox score ?
86
PDB code
2box
Structure name
egf domains 1,2,5 of human emr2, a 7-tm immune system molecule, in complex with strontium
Structure deposition date
2005-04-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UHX3
Residue number A
96
Residue number B
117
Peptide name
Adhesion G protein-coupled receptor E2
Ligandability
Cysteine 96 of Adhesion G protein-coupled receptor E2
Cysteine 117 of Adhesion G protein-coupled receptor E2
2box A 9 A 21
A redox-regulated disulphide may form within Adhesion G protein-coupled receptor E2 between cysteines 33 and 45 (9 and 21 respectively in this structure).
Details
Redox score ?
86
PDB code
2box
Structure name
egf domains 1,2,5 of human emr2, a 7-tm immune system molecule, in complex with strontium
Structure deposition date
2005-04-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UHX3
Residue number A
33
Residue number B
45
Peptide name
Adhesion G protein-coupled receptor E2
Ligandability
Cysteine 33 of Adhesion G protein-coupled receptor E2
Cysteine 45 of Adhesion G protein-coupled receptor E2
2bo2 A 55 A 70
A redox-regulated disulphide may form within Adhesion G protein-coupled receptor E2 between cysteines 79 and 94 (55 and 70 respectively in this structure).
Details
Redox score ?
86
PDB code
2bo2
Structure name
egf domains 1,2,5 of human emr2, a 7-tm immune system molecule, in complex with calcium
Structure deposition date
2005-04-07
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UHX3
Residue number A
79
Residue number B
94
Peptide name
Adhesion G protein-coupled receptor E2
Ligandability
Cysteine 79 of Adhesion G protein-coupled receptor E2
Cysteine 94 of Adhesion G protein-coupled receptor E2
2bou A 106 A 121
A redox-regulated disulphide may form within Adhesion G protein-coupled receptor E2 between cysteines 223 and 238 (106 and 121 respectively in this structure).
Details
Redox score ?
86
PDB code
2bou
Structure name
egf domains 1,2,5 of human emr2, a 7-tm immune system molecule, in complex with barium
Structure deposition date
2005-04-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UHX3
Residue number A
223
Residue number B
238
Peptide name
Adhesion G protein-coupled receptor E2
Ligandability
Cysteine 223 of Adhesion G protein-coupled receptor E2
Cysteine 238 of Adhesion G protein-coupled receptor E2
2box A 99 A 112
A redox-regulated disulphide may form within Adhesion G protein-coupled receptor E2 between cysteines 216 and 229 (99 and 112 respectively in this structure).
Details
Redox score ?
85
PDB code
2box
Structure name
egf domains 1,2,5 of human emr2, a 7-tm immune system molecule, in complex with strontium
Structure deposition date
2005-04-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UHX3
Residue number A
216
Residue number B
229
Peptide name
Adhesion G protein-coupled receptor E2
Ligandability
Cysteine 216 of Adhesion G protein-coupled receptor E2
Cysteine 229 of Adhesion G protein-coupled receptor E2
2bo2 B 123 B 142
A redox-regulated disulphide may form within Adhesion G protein-coupled receptor E2 between cysteines 240 and 259 (123 and 142 respectively in this structure).
Details
Redox score ?
85
PDB code
2bo2
Structure name
egf domains 1,2,5 of human emr2, a 7-tm immune system molecule, in complex with calcium
Structure deposition date
2005-04-07
Thiol separation (Å)
2
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UHX3
Residue number A
240
Residue number B
259
Peptide name
Adhesion G protein-coupled receptor E2
Ligandability
Cysteine 240 of Adhesion G protein-coupled receptor E2
Cysteine 259 of Adhesion G protein-coupled receptor E2
2box A 106 A 112
A redox-regulated disulphide may form within Adhesion G protein-coupled receptor E2 between cysteines 223 and 229 (106 and 112 respectively in this structure).
Details
Redox score ?
73
PDB code
2box
Structure name
egf domains 1,2,5 of human emr2, a 7-tm immune system molecule, in complex with strontium
Structure deposition date
2005-04-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UHX3
Residue number A
223
Residue number B
229
Peptide name
Adhesion G protein-coupled receptor E2
Ligandability
Cysteine 223 of Adhesion G protein-coupled receptor E2
Cysteine 229 of Adhesion G protein-coupled receptor E2
2bo2 A 55 A 61
A redox-regulated disulphide may form within Adhesion G protein-coupled receptor E2 between cysteines 79 and 85 (55 and 61 respectively in this structure).
Details
Redox score ?
73
PDB code
2bo2
Structure name
egf domains 1,2,5 of human emr2, a 7-tm immune system molecule, in complex with calcium
Structure deposition date
2005-04-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UHX3
Residue number A
79
Residue number B
85
Peptide name
Adhesion G protein-coupled receptor E2
Ligandability
Cysteine 79 of Adhesion G protein-coupled receptor E2
Cysteine 85 of Adhesion G protein-coupled receptor E2
2bou A 9 A 15
A redox-regulated disulphide may form within Adhesion G protein-coupled receptor E2 between cysteines 33 and 39 (9 and 15 respectively in this structure).
Details
Redox score ?
67
PDB code
2bou
Structure name
egf domains 1,2,5 of human emr2, a 7-tm immune system molecule, in complex with barium
Structure deposition date
2005-04-14
Thiol separation (Å)
5
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UHX3
Residue number A
33
Residue number B
39
Peptide name
Adhesion G protein-coupled receptor E2
Ligandability
Cysteine 33 of Adhesion G protein-coupled receptor E2
Cysteine 39 of Adhesion G protein-coupled receptor E2
2bou A 61 A 70
A redox-regulated disulphide may form within Adhesion G protein-coupled receptor E2 between cysteines 85 and 94 (61 and 70 respectively in this structure).
Details
Redox score ?
67
PDB code
2bou
Structure name
egf domains 1,2,5 of human emr2, a 7-tm immune system molecule, in complex with barium
Structure deposition date
2005-04-14
Thiol separation (Å)
5
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UHX3
Residue number A
85
Residue number B
94
Peptide name
Adhesion G protein-coupled receptor E2
Ligandability
Cysteine 85 of Adhesion G protein-coupled receptor E2
Cysteine 94 of Adhesion G protein-coupled receptor E2
2bo2 A 99 A 106
A redox-regulated disulphide may form within Adhesion G protein-coupled receptor E2 between cysteines 216 and 223 (99 and 106 respectively in this structure).
Details
Redox score ?
65
PDB code
2bo2
Structure name
egf domains 1,2,5 of human emr2, a 7-tm immune system molecule, in complex with calcium
Structure deposition date
2005-04-07
Thiol separation (Å)
6
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UHX3
Residue number A
216
Residue number B
223
Peptide name
Adhesion G protein-coupled receptor E2
Ligandability
Cysteine 216 of Adhesion G protein-coupled receptor E2
Cysteine 223 of Adhesion G protein-coupled receptor E2
2box A 5 A 9
A redox-regulated disulphide may form within Adhesion G protein-coupled receptor E2 between cysteines 29 and 33 (5 and 9 respectively in this structure).
Details
Redox score ?
65
PDB code
2box
Structure name
egf domains 1,2,5 of human emr2, a 7-tm immune system molecule, in complex with strontium
Structure deposition date
2005-04-14
Thiol separation (Å)
6
Half-sphere exposure sum ?
44
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UHX3
Residue number A
29
Residue number B
33
Peptide name
Adhesion G protein-coupled receptor E2
Ligandability
Cysteine 29 of Adhesion G protein-coupled receptor E2
Cysteine 33 of Adhesion G protein-coupled receptor E2
2box A 47 A 55
A redox-regulated disulphide may form within Adhesion G protein-coupled receptor E2 between cysteines 71 and 79 (47 and 55 respectively in this structure).
Details
Redox score ?
65
PDB code
2box
Structure name
egf domains 1,2,5 of human emr2, a 7-tm immune system molecule, in complex with strontium
Structure deposition date
2005-04-14
Thiol separation (Å)
6
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UHX3
Residue number A
71
Residue number B
79
Peptide name
Adhesion G protein-coupled receptor E2
Ligandability
Cysteine 71 of Adhesion G protein-coupled receptor E2
Cysteine 79 of Adhesion G protein-coupled receptor E2
2box A 112 A 121
A redox-regulated disulphide may form within Adhesion G protein-coupled receptor E2 between cysteines 229 and 238 (112 and 121 respectively in this structure).
Details
Redox score ?
62
PDB code
2box
Structure name
egf domains 1,2,5 of human emr2, a 7-tm immune system molecule, in complex with strontium
Structure deposition date
2005-04-14
Thiol separation (Å)
6
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UHX3
Residue number A
229
Residue number B
238
Peptide name
Adhesion G protein-coupled receptor E2
Ligandability
Cysteine 229 of Adhesion G protein-coupled receptor E2
Cysteine 238 of Adhesion G protein-coupled receptor E2
2bo2 B 47 B 70
A redox-regulated disulphide may form within Adhesion G protein-coupled receptor E2 between cysteines 71 and 94 (47 and 70 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
2bo2
Structure name
egf domains 1,2,5 of human emr2, a 7-tm immune system molecule, in complex with calcium
Structure deposition date
2005-04-07
Thiol separation (Å)
7
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UHX3
Residue number A
71
Residue number B
94
Peptide name
Adhesion G protein-coupled receptor E2
Ligandability
Cysteine 71 of Adhesion G protein-coupled receptor E2
Cysteine 94 of Adhesion G protein-coupled receptor E2
2box A 15 A 21
A redox-regulated disulphide may form within Adhesion G protein-coupled receptor E2 between cysteines 39 and 45 (15 and 21 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
2box
Structure name
egf domains 1,2,5 of human emr2, a 7-tm immune system molecule, in complex with strontium
Structure deposition date
2005-04-14
Thiol separation (Å)
7
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UHX3
Residue number A
39
Residue number B
45
Peptide name
Adhesion G protein-coupled receptor E2
Ligandability
Cysteine 39 of Adhesion G protein-coupled receptor E2
Cysteine 45 of Adhesion G protein-coupled receptor E2
2box A 5 A 21
A redox-regulated disulphide may form within Adhesion G protein-coupled receptor E2 between cysteines 29 and 45 (5 and 21 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
54
PDB code
2box
Structure name
egf domains 1,2,5 of human emr2, a 7-tm immune system molecule, in complex with strontium
Structure deposition date
2005-04-14
Thiol separation (Å)
8
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UHX3
Residue number A
29
Residue number B
45
Peptide name
Adhesion G protein-coupled receptor E2
Ligandability
Cysteine 29 of Adhesion G protein-coupled receptor E2
Cysteine 45 of Adhesion G protein-coupled receptor E2
2bou A 99 A 121
A redox-regulated disulphide may form within Adhesion G protein-coupled receptor E2 between cysteines 216 and 238 (99 and 121 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
53
PDB code
2bou
Structure name
egf domains 1,2,5 of human emr2, a 7-tm immune system molecule, in complex with barium
Structure deposition date
2005-04-14
Thiol separation (Å)
8
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UHX3
Residue number A
216
Residue number B
238
Peptide name
Adhesion G protein-coupled receptor E2
Ligandability
Cysteine 216 of Adhesion G protein-coupled receptor E2
Cysteine 238 of Adhesion G protein-coupled receptor E2
2box A 21 A 41
A redox-regulated disulphide may form within Adhesion G protein-coupled receptor E2 between cysteines 45 and 65 (21 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 ?
52
PDB code
2box
Structure name
egf domains 1,2,5 of human emr2, a 7-tm immune system molecule, in complex with strontium
Structure deposition date
2005-04-14
Thiol separation (Å)
8
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UHX3
Residue number A
45
Residue number B
65
Peptide name
Adhesion G protein-coupled receptor E2
Ligandability
Cysteine 45 of Adhesion G protein-coupled receptor E2
Cysteine 65 of Adhesion G protein-coupled receptor E2
2bo2 A 55 A 93
A redox-regulated disulphide may form within Adhesion G protein-coupled receptor E2 between cysteines 79 and 117 (55 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 ?
49
PDB code
2bo2
Structure name
egf domains 1,2,5 of human emr2, a 7-tm immune system molecule, in complex with calcium
Structure deposition date
2005-04-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UHX3
Residue number A
79
Residue number B
117
Peptide name
Adhesion G protein-coupled receptor E2
Ligandability
Cysteine 79 of Adhesion G protein-coupled receptor E2
Cysteine 117 of Adhesion G protein-coupled receptor E2
2bo2 A 70 A 93
A redox-regulated disulphide may form within Adhesion G protein-coupled receptor E2 between cysteines 94 and 117 (70 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 ?
48
PDB code
2bo2
Structure name
egf domains 1,2,5 of human emr2, a 7-tm immune system molecule, in complex with calcium
Structure deposition date
2005-04-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UHX3
Residue number A
94
Residue number B
117
Peptide name
Adhesion G protein-coupled receptor E2
Ligandability
Cysteine 94 of Adhesion G protein-coupled receptor E2
Cysteine 117 of Adhesion G protein-coupled receptor E2
2bo2 A 9 A 41
A redox-regulated disulphide may form within Adhesion G protein-coupled receptor E2 between cysteines 33 and 65 (9 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 ?
47
PDB code
2bo2
Structure name
egf domains 1,2,5 of human emr2, a 7-tm immune system molecule, in complex with calcium
Structure deposition date
2005-04-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UHX3
Residue number A
33
Residue number B
65
Peptide name
Adhesion G protein-coupled receptor E2
Ligandability
Cysteine 33 of Adhesion G protein-coupled receptor E2
Cysteine 65 of Adhesion G protein-coupled receptor E2
2box A 121 A 142
A redox-regulated disulphide may form within Adhesion G protein-coupled receptor E2 between cysteines 238 and 259 (121 and 142 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
2box
Structure name
egf domains 1,2,5 of human emr2, a 7-tm immune system molecule, in complex with strontium
Structure deposition date
2005-04-14
Thiol separation (Å)
9
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UHX3
Residue number A
238
Residue number B
259
Peptide name
Adhesion G protein-coupled receptor E2
Ligandability
Cysteine 238 of Adhesion G protein-coupled receptor E2
Cysteine 259 of Adhesion G protein-coupled receptor E2
2bo2 A 106 A 142
A redox-regulated disulphide may form within Adhesion G protein-coupled receptor E2 between cysteines 223 and 259 (106 and 142 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
2bo2
Structure name
egf domains 1,2,5 of human emr2, a 7-tm immune system molecule, in complex with calcium
Structure deposition date
2005-04-07
Thiol separation (Å)
10
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UHX3
Residue number A
223
Residue number B
259
Peptide name
Adhesion G protein-coupled receptor E2
Ligandability
Cysteine 223 of Adhesion G protein-coupled receptor E2
Cysteine 259 of Adhesion G protein-coupled receptor E2
2box A 21 A 23
A redox-regulated disulphide may form within Adhesion G protein-coupled receptor E2 between cysteines 45 and 47 (21 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 ?
45
PDB code
2box
Structure name
egf domains 1,2,5 of human emr2, a 7-tm immune system molecule, in complex with strontium
Structure deposition date
2005-04-14
Thiol separation (Å)
9
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UHX3
Residue number A
45
Residue number B
47
Peptide name
Adhesion G protein-coupled receptor E2
Ligandability
Cysteine 45 of Adhesion G protein-coupled receptor E2
Cysteine 47 of Adhesion G protein-coupled receptor E2
2box A 121 A 123
A redox-regulated disulphide may form within Adhesion G protein-coupled receptor E2 between cysteines 238 and 240 (121 and 123 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
2box
Structure name
egf domains 1,2,5 of human emr2, a 7-tm immune system molecule, in complex with strontium
Structure deposition date
2005-04-14
Thiol separation (Å)
10
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UHX3
Residue number A
238
Residue number B
240
Peptide name
Adhesion G protein-coupled receptor E2
Ligandability
Cysteine 238 of Adhesion G protein-coupled receptor E2
Cysteine 240 of Adhesion G protein-coupled receptor E2
2bo2 B 55 B 72
A redox-regulated disulphide may form within Adhesion G protein-coupled receptor E2 between cysteines 79 and 96 (55 and 72 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
2bo2
Structure name
egf domains 1,2,5 of human emr2, a 7-tm immune system molecule, in complex with calcium
Structure deposition date
2005-04-07
Thiol separation (Å)
10
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UHX3
Residue number A
79
Residue number B
96
Peptide name
Adhesion G protein-coupled receptor E2
Ligandability
Cysteine 79 of Adhesion G protein-coupled receptor E2
Cysteine 96 of Adhesion G protein-coupled receptor E2
2bou A 70 A 72
A redox-regulated disulphide may form within Adhesion G protein-coupled receptor E2 between cysteines 94 and 96 (70 and 72 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
2bou
Structure name
egf domains 1,2,5 of human emr2, a 7-tm immune system molecule, in complex with barium
Structure deposition date
2005-04-14
Thiol separation (Å)
9
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UHX3
Residue number A
94
Residue number B
96
Peptide name
Adhesion G protein-coupled receptor E2
Ligandability
Cysteine 94 of Adhesion G protein-coupled receptor E2
Cysteine 96 of Adhesion G protein-coupled receptor E2
2bou A 9 A 23
A redox-regulated disulphide may form within Adhesion G protein-coupled receptor E2 between cysteines 33 and 47 (9 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 ?
42
PDB code
2bou
Structure name
egf domains 1,2,5 of human emr2, a 7-tm immune system molecule, in complex with barium
Structure deposition date
2005-04-14
Thiol separation (Å)
10
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UHX3
Residue number A
33
Residue number B
47
Peptide name
Adhesion G protein-coupled receptor E2
Ligandability
Cysteine 33 of Adhesion G protein-coupled receptor E2
Cysteine 47 of Adhesion G protein-coupled receptor E2
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