Glycoprotein hormones alpha chain
Intermolecular
Cysteine 31 and cysteine 102 of Follitropin subunit beta
Cysteine 31 and cysteine 50 of Follitropin subunit beta
Cysteine 55 and cysteine 102 of Follitropin subunit beta
Cysteine 55 and cysteine 50 of Follitropin subunit beta
Cysteine 111 and cysteine 105 of Follitropin subunit beta
Cysteine 31 and cysteine 21 of Follitropin subunit beta
Cysteine 111 and cysteine 50 of Follitropin subunit beta
Cysteine 83 and cysteine 50 of Follitropin subunit beta
Cysteine 31 and cysteine 69 of Follitropin subunit beta
Cysteine 111 and cysteine 112 of Follitropin subunit beta
More...Cysteine 56 and cysteine 50 of Follitropin subunit beta
Intramolecular
Cysteine 52 and cysteine 106
Cysteine 31 and cysteine 55
Cysteine 34 and cysteine 84
Cysteine 56 and cysteine 108
Cysteine 83 and cysteine 111
Cysteine 34 and cysteine 108
Cysteine 34 and cysteine 106
Cysteine 34 and cysteine 56
Cysteine 84 and cysteine 106
Cysteine 34 and cysteine 52
Cysteine 56 and cysteine 84
Cysteine 52 and cysteine 84
Cysteine 84 and cysteine 108
Cysteine 56 and cysteine 111
Cysteine 56 and cysteine 83
Cysteine 55 and cysteine 56
Cysteine 108 and cysteine 111
Cysteine 31 and cysteine 56
Cysteine 106 and cysteine 108
Cysteine 34 and cysteine 55
Cysteine 83 and cysteine 108
Cysteine 55 and cysteine 108
Cysteine 31 and cysteine 108
Cysteine 55 and cysteine 84
Cysteine 56 and cysteine 106
Cysteine 34 and cysteine 83
Cysteine 52 and cysteine 108
Cysteine 83 and cysteine 84
Cysteine 52 and cysteine 56
4ay9 A 7 B 84
A redox-regulated disulphide may form between cysteine 31 of Glycoprotein hormones alpha chain and cysteine 102 of Follitropin subunit beta (7 and 84 respectively in this structure).
Details
Redox score ?
61
PDB code
4ay9
Structure name
structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor
Structure deposition date
2012-06-19
Thiol separation (Å)
7
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide A name
Glycoprotein hormones alpha chain
Peptide B name
Follitropin subunit beta
Peptide A accession
Q96QJ4
Peptide B accession
P01225
Peptide A residue number
31
Peptide B residue number
102
Ligandability
Cysteine 31 of Glycoprotein hormones alpha chain
Cysteine 102 of Follitropin subunit beta
4mqw A 7 B 32
A redox-regulated disulphide may form between cysteine 31 of Glycoprotein hormones alpha chain and cysteine 50 of Follitropin subunit beta (7 and 32 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
57
PDB code
4mqw
Structure name
structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor (p31)
Structure deposition date
2013-09-16
Thiol separation (Å)
7
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide A name
Glycoprotein hormones alpha chain
Peptide B name
Follitropin subunit beta
Peptide A accession
Q96QJ4
Peptide B accession
P01225
Peptide A residue number
31
Peptide B residue number
50
Ligandability
Cysteine 31 of Glycoprotein hormones alpha chain
Cysteine 50 of Follitropin subunit beta
4mqw G 31 H 84
A redox-regulated disulphide may form between cysteine 55 of Glycoprotein hormones alpha chain and cysteine 102 of Follitropin subunit beta (31 and 84 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
4mqw
Structure name
structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor (p31)
Structure deposition date
2013-09-16
Thiol separation (Å)
8
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide A name
Glycoprotein hormones alpha chain
Peptide B name
Follitropin subunit beta
Peptide A accession
Q96QJ4
Peptide B accession
P01225
Peptide A residue number
55
Peptide B residue number
102
Ligandability
Cysteine 55 of Glycoprotein hormones alpha chain
Cysteine 102 of Follitropin subunit beta
4mqw G 31 H 32
A redox-regulated disulphide may form between cysteine 55 of Glycoprotein hormones alpha chain and cysteine 50 of Follitropin subunit beta (31 and 32 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
4mqw
Structure name
structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor (p31)
Structure deposition date
2013-09-16
Thiol separation (Å)
8
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide A name
Glycoprotein hormones alpha chain
Peptide B name
Follitropin subunit beta
Peptide A accession
Q96QJ4
Peptide B accession
P01225
Peptide A residue number
55
Peptide B residue number
50
Ligandability
Cysteine 55 of Glycoprotein hormones alpha chain
Cysteine 50 of Follitropin subunit beta
4ay9 G 87 H 87
A redox-regulated disulphide may form between cysteine 111 of Glycoprotein hormones alpha chain and cysteine 105 of Follitropin subunit beta (87 and 87 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
4ay9
Structure name
structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor
Structure deposition date
2012-06-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide A name
Glycoprotein hormones alpha chain
Peptide B name
Follitropin subunit beta
Peptide A accession
Q96QJ4
Peptide B accession
P01225
Peptide A residue number
111
Peptide B residue number
105
Ligandability
Cysteine 111 of Glycoprotein hormones alpha chain
Cysteine 105 of Follitropin subunit beta
4ay9 D 7 E 3
A redox-regulated disulphide may form between cysteine 31 of Glycoprotein hormones alpha chain and cysteine 21 of Follitropin subunit beta (7 and 3 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
4ay9
Structure name
structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor
Structure deposition date
2012-06-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide A name
Glycoprotein hormones alpha chain
Peptide B name
Follitropin subunit beta
Peptide A accession
Q96QJ4
Peptide B accession
P01225
Peptide A residue number
31
Peptide B residue number
21
Ligandability
Cysteine 31 of Glycoprotein hormones alpha chain
Cysteine 21 of Follitropin subunit beta
4ay9 A 87 B 32
A redox-regulated disulphide may form between cysteine 111 of Glycoprotein hormones alpha chain and cysteine 50 of Follitropin subunit beta (87 and 32 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
4ay9
Structure name
structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor
Structure deposition date
2012-06-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide A name
Glycoprotein hormones alpha chain
Peptide B name
Follitropin subunit beta
Peptide A accession
Q96QJ4
Peptide B accession
P01225
Peptide A residue number
111
Peptide B residue number
50
Ligandability
Cysteine 111 of Glycoprotein hormones alpha chain
Cysteine 50 of Follitropin subunit beta
4mqw G 59 H 32
A redox-regulated disulphide may form between cysteine 83 of Glycoprotein hormones alpha chain and cysteine 50 of Follitropin subunit beta (59 and 32 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
4mqw
Structure name
structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor (p31)
Structure deposition date
2013-09-16
Thiol separation (Å)
8
Half-sphere exposure sum ?
83
Minimum pKa ?
nan
% buried
nan
Peptide A name
Glycoprotein hormones alpha chain
Peptide B name
Follitropin subunit beta
Peptide A accession
Q96QJ4
Peptide B accession
P01225
Peptide A residue number
83
Peptide B residue number
50
Ligandability
Cysteine 83 of Glycoprotein hormones alpha chain
Cysteine 50 of Follitropin subunit beta
4mqw A 7 B 51
A redox-regulated disulphide may form between cysteine 31 of Glycoprotein hormones alpha chain and cysteine 69 of Follitropin subunit beta (7 and 51 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
4mqw
Structure name
structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor (p31)
Structure deposition date
2013-09-16
Thiol separation (Å)
10
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide A name
Glycoprotein hormones alpha chain
Peptide B name
Follitropin subunit beta
Peptide A accession
Q96QJ4
Peptide B accession
P01225
Peptide A residue number
31
Peptide B residue number
69
Ligandability
Cysteine 31 of Glycoprotein hormones alpha chain
Cysteine 69 of Follitropin subunit beta
4ay9 G 87 H 94
A redox-regulated disulphide may form between cysteine 111 of Glycoprotein hormones alpha chain and cysteine 112 of Follitropin subunit beta (87 and 94 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
4ay9
Structure name
structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor
Structure deposition date
2012-06-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide A name
Glycoprotein hormones alpha chain
Peptide B name
Follitropin subunit beta
Peptide A accession
Q96QJ4
Peptide B accession
P01225
Peptide A residue number
111
Peptide B residue number
112
Ligandability
Cysteine 111 of Glycoprotein hormones alpha chain
Cysteine 112 of Follitropin subunit beta
4ay9 D 32 E 32
A redox-regulated disulphide may form between cysteine 56 of Glycoprotein hormones alpha chain and cysteine 50 of Follitropin subunit beta (32 and 32 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
4ay9
Structure name
structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor
Structure deposition date
2012-06-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide A name
Glycoprotein hormones alpha chain
Peptide B name
Follitropin subunit beta
Peptide A accession
Q96QJ4
Peptide B accession
P01225
Peptide A residue number
56
Peptide B residue number
50
Ligandability
Cysteine 56 of Glycoprotein hormones alpha chain
Cysteine 50 of Follitropin subunit beta
4mqw A 28 A 82
A redox-regulated disulphide may form within Glycoprotein hormones alpha chain between cysteines 52 and 106 (28 and 82 respectively in this structure).
Details
Redox score ?
85
PDB code
4mqw
Structure name
structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor (p31)
Structure deposition date
2013-09-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96QJ4
Residue number A
52
Residue number B
106
Peptide name
Glycoprotein hormones alpha chain
Ligandability
Cysteine 52 of Glycoprotein hormones alpha chain
Cysteine 106 of Glycoprotein hormones alpha chain
4ay9 G 7 G 31
A redox-regulated disulphide may form within Glycoprotein hormones alpha chain between cysteines 31 and 55 (7 and 31 respectively in this structure).
Details
Redox score ?
85
PDB code
4ay9
Structure name
structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor
Structure deposition date
2012-06-19
Thiol separation (Å)
2
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96QJ4
Residue number A
31
Residue number B
55
Peptide name
Glycoprotein hormones alpha chain
Ligandability
Cysteine 31 of Glycoprotein hormones alpha chain
Cysteine 55 of Glycoprotein hormones alpha chain
4mqw A 10 A 60
A redox-regulated disulphide may form within Glycoprotein hormones alpha chain between cysteines 34 and 84 (10 and 60 respectively in this structure).
Details
Redox score ?
85
PDB code
4mqw
Structure name
structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor (p31)
Structure deposition date
2013-09-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96QJ4
Residue number A
34
Residue number B
84
Peptide name
Glycoprotein hormones alpha chain
Ligandability
Cysteine 34 of Glycoprotein hormones alpha chain
Cysteine 84 of Glycoprotein hormones alpha chain
4mqw G 32 G 84
A redox-regulated disulphide may form within Glycoprotein hormones alpha chain between cysteines 56 and 108 (32 and 84 respectively in this structure).
Details
Redox score ?
83
PDB code
4mqw
Structure name
structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor (p31)
Structure deposition date
2013-09-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96QJ4
Residue number A
56
Residue number B
108
Peptide name
Glycoprotein hormones alpha chain
Ligandability
Cysteine 56 of Glycoprotein hormones alpha chain
Cysteine 108 of Glycoprotein hormones alpha chain
4mqw G 59 G 87
A redox-regulated disulphide may form within Glycoprotein hormones alpha chain between cysteines 83 and 111 (59 and 87 respectively in this structure).
Details
Redox score ?
83
PDB code
4mqw
Structure name
structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor (p31)
Structure deposition date
2013-09-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96QJ4
Residue number A
83
Residue number B
111
Peptide name
Glycoprotein hormones alpha chain
Ligandability
Cysteine 83 of Glycoprotein hormones alpha chain
Cysteine 111 of Glycoprotein hormones alpha chain
4mqw D 10 D 84
A redox-regulated disulphide may form within Glycoprotein hormones alpha chain between cysteines 34 and 108 (10 and 84 respectively in this structure).
Details
Redox score ?
74
PDB code
4mqw
Structure name
structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor (p31)
Structure deposition date
2013-09-16
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96QJ4
Residue number A
34
Residue number B
108
Peptide name
Glycoprotein hormones alpha chain
Ligandability
Cysteine 34 of Glycoprotein hormones alpha chain
Cysteine 108 of Glycoprotein hormones alpha chain
4mqw A 10 A 82
A redox-regulated disulphide may form within Glycoprotein hormones alpha chain between cysteines 34 and 106 (10 and 82 respectively in this structure).
Details
Redox score ?
72
PDB code
4mqw
Structure name
structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor (p31)
Structure deposition date
2013-09-16
Thiol separation (Å)
5
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96QJ4
Residue number A
34
Residue number B
106
Peptide name
Glycoprotein hormones alpha chain
Ligandability
Cysteine 34 of Glycoprotein hormones alpha chain
Cysteine 106 of Glycoprotein hormones alpha chain
4ay9 G 10 G 32
A redox-regulated disulphide may form within Glycoprotein hormones alpha chain between cysteines 34 and 56 (10 and 32 respectively in this structure).
Details
Redox score ?
70
PDB code
4ay9
Structure name
structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor
Structure deposition date
2012-06-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96QJ4
Residue number A
34
Residue number B
56
Peptide name
Glycoprotein hormones alpha chain
Ligandability
Cysteine 34 of Glycoprotein hormones alpha chain
Cysteine 56 of Glycoprotein hormones alpha chain
4mqw D 60 D 82
A redox-regulated disulphide may form within Glycoprotein hormones alpha chain between cysteines 84 and 106 (60 and 82 respectively in this structure).
Details
Redox score ?
66
PDB code
4mqw
Structure name
structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor (p31)
Structure deposition date
2013-09-16
Thiol separation (Å)
5
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96QJ4
Residue number A
84
Residue number B
106
Peptide name
Glycoprotein hormones alpha chain
Ligandability
Cysteine 84 of Glycoprotein hormones alpha chain
Cysteine 106 of Glycoprotein hormones alpha chain
4ay9 A 10 A 28
A redox-regulated disulphide may form within Glycoprotein hormones alpha chain between cysteines 34 and 52 (10 and 28 respectively in this structure).
Details
Redox score ?
66
PDB code
4ay9
Structure name
structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor
Structure deposition date
2012-06-19
Thiol separation (Å)
5
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96QJ4
Residue number A
34
Residue number B
52
Peptide name
Glycoprotein hormones alpha chain
Ligandability
Cysteine 34 of Glycoprotein hormones alpha chain
Cysteine 52 of Glycoprotein hormones alpha chain
4mqw G 32 G 60
A redox-regulated disulphide may form within Glycoprotein hormones alpha chain between cysteines 56 and 84 (32 and 60 respectively in this structure).
Details
Redox score ?
63
PDB code
4mqw
Structure name
structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor (p31)
Structure deposition date
2013-09-16
Thiol separation (Å)
5
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96QJ4
Residue number A
56
Residue number B
84
Peptide name
Glycoprotein hormones alpha chain
Ligandability
Cysteine 56 of Glycoprotein hormones alpha chain
Cysteine 84 of Glycoprotein hormones alpha chain
4ay9 D 28 D 60
A redox-regulated disulphide may form within Glycoprotein hormones alpha chain between cysteines 52 and 84 (28 and 60 respectively in this structure).
Details
Redox score ?
63
PDB code
4ay9
Structure name
structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor
Structure deposition date
2012-06-19
Thiol separation (Å)
5
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96QJ4
Residue number A
52
Residue number B
84
Peptide name
Glycoprotein hormones alpha chain
Ligandability
Cysteine 52 of Glycoprotein hormones alpha chain
Cysteine 84 of Glycoprotein hormones alpha chain
4ay9 D 60 D 84
A redox-regulated disulphide may form within Glycoprotein hormones alpha chain between cysteines 84 and 108 (60 and 84 respectively in this structure).
Details
Redox score ?
61
PDB code
4ay9
Structure name
structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor
Structure deposition date
2012-06-19
Thiol separation (Å)
6
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96QJ4
Residue number A
84
Residue number B
108
Peptide name
Glycoprotein hormones alpha chain
Ligandability
Cysteine 84 of Glycoprotein hormones alpha chain
Cysteine 108 of Glycoprotein hormones alpha chain
4ay9 G 32 G 87
A redox-regulated disulphide may form within Glycoprotein hormones alpha chain between cysteines 56 and 111 (32 and 87 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
4ay9
Structure name
structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor
Structure deposition date
2012-06-19
Thiol separation (Å)
7
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96QJ4
Residue number A
56
Residue number B
111
Peptide name
Glycoprotein hormones alpha chain
Ligandability
Cysteine 56 of Glycoprotein hormones alpha chain
Cysteine 111 of Glycoprotein hormones alpha chain
4mqw A 32 A 59
A redox-regulated disulphide may form within Glycoprotein hormones alpha chain between cysteines 56 and 83 (32 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 ?
51
PDB code
4mqw
Structure name
structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor (p31)
Structure deposition date
2013-09-16
Thiol separation (Å)
7
Half-sphere exposure sum ?
84
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96QJ4
Residue number A
56
Residue number B
83
Peptide name
Glycoprotein hormones alpha chain
Ligandability
Cysteine 56 of Glycoprotein hormones alpha chain
Cysteine 83 of Glycoprotein hormones alpha chain
4ay9 A 31 A 32
A redox-regulated disulphide may form within Glycoprotein hormones alpha chain between cysteines 55 and 56 (31 and 32 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
4ay9
Structure name
structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor
Structure deposition date
2012-06-19
Thiol separation (Å)
7
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96QJ4
Residue number A
55
Residue number B
56
Peptide name
Glycoprotein hormones alpha chain
Ligandability
Cysteine 55 of Glycoprotein hormones alpha chain
Cysteine 56 of Glycoprotein hormones alpha chain
4mqw A 84 A 87
A redox-regulated disulphide may form within Glycoprotein hormones alpha chain between cysteines 108 and 111 (84 and 87 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
4mqw
Structure name
structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor (p31)
Structure deposition date
2013-09-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96QJ4
Residue number A
108
Residue number B
111
Peptide name
Glycoprotein hormones alpha chain
Ligandability
Cysteine 108 of Glycoprotein hormones alpha chain
Cysteine 111 of Glycoprotein hormones alpha chain
4ay9 D 7 D 32
A redox-regulated disulphide may form within Glycoprotein hormones alpha chain between cysteines 31 and 56 (7 and 32 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
4ay9
Structure name
structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor
Structure deposition date
2012-06-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96QJ4
Residue number A
31
Residue number B
56
Peptide name
Glycoprotein hormones alpha chain
Ligandability
Cysteine 31 of Glycoprotein hormones alpha chain
Cysteine 56 of Glycoprotein hormones alpha chain
4mqw A 82 A 84
A redox-regulated disulphide may form within Glycoprotein hormones alpha chain between cysteines 106 and 108 (82 and 84 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
4mqw
Structure name
structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor (p31)
Structure deposition date
2013-09-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96QJ4
Residue number A
106
Residue number B
108
Peptide name
Glycoprotein hormones alpha chain
Ligandability
Cysteine 106 of Glycoprotein hormones alpha chain
Cysteine 108 of Glycoprotein hormones alpha chain
4ay9 A 10 A 31
A redox-regulated disulphide may form within Glycoprotein hormones alpha chain between cysteines 34 and 55 (10 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
4ay9
Structure name
structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor
Structure deposition date
2012-06-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96QJ4
Residue number A
34
Residue number B
55
Peptide name
Glycoprotein hormones alpha chain
Ligandability
Cysteine 34 of Glycoprotein hormones alpha chain
Cysteine 55 of Glycoprotein hormones alpha chain
4mqw A 59 A 84
A redox-regulated disulphide may form within Glycoprotein hormones alpha chain between cysteines 83 and 108 (59 and 84 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
4mqw
Structure name
structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor (p31)
Structure deposition date
2013-09-16
Thiol separation (Å)
8
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96QJ4
Residue number A
83
Residue number B
108
Peptide name
Glycoprotein hormones alpha chain
Ligandability
Cysteine 83 of Glycoprotein hormones alpha chain
Cysteine 108 of Glycoprotein hormones alpha chain
4mqw G 31 G 84
A redox-regulated disulphide may form within Glycoprotein hormones alpha chain between cysteines 55 and 108 (31 and 84 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
4mqw
Structure name
structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor (p31)
Structure deposition date
2013-09-16
Thiol separation (Å)
8
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96QJ4
Residue number A
55
Residue number B
108
Peptide name
Glycoprotein hormones alpha chain
Ligandability
Cysteine 55 of Glycoprotein hormones alpha chain
Cysteine 108 of Glycoprotein hormones alpha chain
4ay9 D 7 D 84
A redox-regulated disulphide may form within Glycoprotein hormones alpha chain between cysteines 31 and 108 (7 and 84 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
4ay9
Structure name
structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor
Structure deposition date
2012-06-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96QJ4
Residue number A
31
Residue number B
108
Peptide name
Glycoprotein hormones alpha chain
Ligandability
Cysteine 31 of Glycoprotein hormones alpha chain
Cysteine 108 of Glycoprotein hormones alpha chain
4ay9 A 31 A 60
A redox-regulated disulphide may form within Glycoprotein hormones alpha chain between cysteines 55 and 84 (31 and 60 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
4ay9
Structure name
structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor
Structure deposition date
2012-06-19
Thiol separation (Å)
8
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96QJ4
Residue number A
55
Residue number B
84
Peptide name
Glycoprotein hormones alpha chain
Ligandability
Cysteine 55 of Glycoprotein hormones alpha chain
Cysteine 84 of Glycoprotein hormones alpha chain
4mqw D 32 D 82
A redox-regulated disulphide may form within Glycoprotein hormones alpha chain between cysteines 56 and 106 (32 and 82 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
4mqw
Structure name
structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor (p31)
Structure deposition date
2013-09-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96QJ4
Residue number A
56
Residue number B
106
Peptide name
Glycoprotein hormones alpha chain
Ligandability
Cysteine 56 of Glycoprotein hormones alpha chain
Cysteine 106 of Glycoprotein hormones alpha chain
4ay9 G 10 G 59
A redox-regulated disulphide may form within Glycoprotein hormones alpha chain between cysteines 34 and 83 (10 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 ?
41
PDB code
4ay9
Structure name
structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor
Structure deposition date
2012-06-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96QJ4
Residue number A
34
Residue number B
83
Peptide name
Glycoprotein hormones alpha chain
Ligandability
Cysteine 34 of Glycoprotein hormones alpha chain
Cysteine 83 of Glycoprotein hormones alpha chain
4mqw A 28 A 84
A redox-regulated disulphide may form within Glycoprotein hormones alpha chain between cysteines 52 and 108 (28 and 84 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
4mqw
Structure name
structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor (p31)
Structure deposition date
2013-09-16
Thiol separation (Å)
10
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96QJ4
Residue number A
52
Residue number B
108
Peptide name
Glycoprotein hormones alpha chain
Ligandability
Cysteine 52 of Glycoprotein hormones alpha chain
Cysteine 108 of Glycoprotein hormones alpha chain
4mqw D 59 D 60
A redox-regulated disulphide may form within Glycoprotein hormones alpha chain between cysteines 83 and 84 (59 and 60 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
4mqw
Structure name
structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor (p31)
Structure deposition date
2013-09-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
83
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96QJ4
Residue number A
83
Residue number B
84
Peptide name
Glycoprotein hormones alpha chain
Ligandability
Cysteine 83 of Glycoprotein hormones alpha chain
Cysteine 84 of Glycoprotein hormones alpha chain
4mqw G 28 G 32
A redox-regulated disulphide may form within Glycoprotein hormones alpha chain between cysteines 52 and 56 (28 and 32 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
4mqw
Structure name
structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor (p31)
Structure deposition date
2013-09-16
Thiol separation (Å)
10
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96QJ4
Residue number A
52
Residue number B
56
Peptide name
Glycoprotein hormones alpha chain
Ligandability
Cysteine 52 of Glycoprotein hormones alpha chain
Cysteine 56 of Glycoprotein hormones alpha chain
If this tool was useful for finding a disulphide, please cite: