Follitropin subunit beta
Intermolecular
Cysteine 31 of Glycoprotein hormones alpha chain and cysteine 102
Cysteine 31 of Glycoprotein hormones alpha chain and cysteine 102
Cysteine 31 of Glycoprotein hormones alpha chain and cysteine 50
Cysteine 31 of Glycoprotein hormones alpha chain and cysteine 50
Cysteine 31 of Glycoprotein hormones alpha chain and cysteine 21
Cysteine 55 of Glycoprotein hormones alpha chain and cysteine 102
Cysteine 55 of Glycoprotein hormones alpha chain and cysteine 50
Cysteine 55 of Glycoprotein hormones alpha chain and cysteine 102
Cysteine 55 of Glycoprotein hormones alpha chain and cysteine 50
Cysteine 111 of Glycoprotein hormones alpha chain and cysteine 105
More...Cysteine 111 of Glycoprotein hormones alpha chain and cysteine 105
Cysteine 31 of Glycoprotein hormones alpha chain and cysteine 21
Cysteine 111 of Glycoprotein hormones alpha chain and cysteine 50
Cysteine 111 of Glycoprotein hormones alpha chain and cysteine 112
Cysteine 83 of Glycoprotein hormones alpha chain and cysteine 50
Cysteine 31 of Glycoprotein hormones alpha chain and cysteine 69
Cysteine 83 of Glycoprotein hormones alpha chain and cysteine 50
Cysteine 31 of Glycoprotein hormones alpha chain and cysteine 69
Cysteine 56 of Glycoprotein hormones alpha chain and cysteine 50
Cysteine 111 of Glycoprotein hormones alpha chain and cysteine 112
Cysteine 111 of Glycoprotein hormones alpha chain and cysteine 50
Cysteine 56 of Glycoprotein hormones alpha chain and cysteine 50
Intramolecular
Cysteine 35 and cysteine 84
Cysteine 46 and cysteine 100
Cysteine 38 and cysteine 122
Cysteine 21 and cysteine 69
Cysteine 105 and cysteine 112
Cysteine 50 and cysteine 102
Cysteine 21 and cysteine 102
Cysteine 21 and cysteine 100
Cysteine 21 and cysteine 46
Cysteine 21 and cysteine 50
Cysteine 69 and cysteine 100
Cysteine 50 and cysteine 69
Cysteine 69 and cysteine 102
Cysteine 46 and cysteine 69
Cysteine 100 and cysteine 102
Cysteine 50 and cysteine 100
Cysteine 46 and cysteine 102
Cysteine 46 and cysteine 50
1fl7 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
1fl7
Structure name
human follicle stimulating hormone
Structure deposition date
2000-08-11
Thiol separation (Å)
7
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide A name
Glycoprotein hormones alpha chain
Peptide B name
Follitropin subunit beta
Peptide A accession
P01215
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
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
1xwd D 7 E 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 ?
59
PDB code
1xwd
Structure name
crystal structure of human follicle stimulating hormone complexed with its receptor
Structure deposition date
2004-10-30
Thiol separation (Å)
7
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide A name
Glycoprotein hormones alpha chain
Peptide B name
Follitropin subunit beta
Peptide A accession
P01215
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 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
1xwd A 7 B 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 ?
51
PDB code
1xwd
Structure name
crystal structure of human follicle stimulating hormone complexed with its receptor
Structure deposition date
2004-10-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide A name
Glycoprotein hormones alpha chain
Peptide B name
Follitropin subunit beta
Peptide A accession
P01215
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
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
1fl7 A 31 B 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 ?
48
PDB code
1fl7
Structure name
human follicle stimulating hormone
Structure deposition date
2000-08-11
Thiol separation (Å)
7
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide A name
Glycoprotein hormones alpha chain
Peptide B name
Follitropin subunit beta
Peptide A accession
P01215
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
1xwd A 31 B 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 ?
47
PDB code
1xwd
Structure name
crystal structure of human follicle stimulating hormone complexed with its receptor
Structure deposition date
2004-10-30
Thiol separation (Å)
8
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
P01215
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
1fl7 A 87 B 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
1fl7
Structure name
human follicle stimulating hormone
Structure deposition date
2000-08-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide A name
Glycoprotein hormones alpha chain
Peptide B name
Follitropin subunit beta
Peptide A accession
P01215
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
1xwd D 87 E 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 ?
41
PDB code
1xwd
Structure name
crystal structure of human follicle stimulating hormone complexed with its receptor
Structure deposition date
2004-10-30
Thiol separation (Å)
9
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
P01215
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
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
1xwd D 7 E 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 ?
40
PDB code
1xwd
Structure name
crystal structure of human follicle stimulating hormone complexed with its receptor
Structure deposition date
2004-10-30
Thiol separation (Å)
10
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide A name
Glycoprotein hormones alpha chain
Peptide B name
Follitropin subunit beta
Peptide A accession
P01215
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
1fl7 C 59 D 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 ?
40
PDB code
1fl7
Structure name
human follicle stimulating hormone
Structure deposition date
2000-08-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide A name
Glycoprotein hormones alpha chain
Peptide B name
Follitropin subunit beta
Peptide A accession
P01215
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
1xwd A 32 B 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 ?
38
PDB code
1xwd
Structure name
crystal structure of human follicle stimulating hormone complexed with its receptor
Structure deposition date
2004-10-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide A name
Glycoprotein hormones alpha chain
Peptide B name
Follitropin subunit beta
Peptide A accession
P01215
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
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
1fl7 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 ?
37
PDB code
1fl7
Structure name
human follicle stimulating hormone
Structure deposition date
2000-08-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide A name
Glycoprotein hormones alpha chain
Peptide B name
Follitropin subunit beta
Peptide A accession
P01215
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
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
1fl7 D 17 D 66
A redox-regulated disulphide may form within Follitropin subunit beta between cysteines 35 and 84 (17 and 66 respectively in this structure).
Details
Redox score ?
87
PDB code
1fl7
Structure name
human follicle stimulating hormone
Structure deposition date
2000-08-11
Thiol separation (Å)
2
Half-sphere exposure sum ?
38
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01225
Residue number A
35
Residue number B
84
Peptide name
Follitropin subunit beta
Ligandability
Cysteine 35 of Follitropin subunit beta
Cysteine 84 of Follitropin subunit beta
4mqw B 28 B 82
A redox-regulated disulphide may form within Follitropin subunit beta between cysteines 46 and 100 (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 ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01225
Residue number A
46
Residue number B
100
Peptide name
Follitropin subunit beta
Ligandability
Cysteine 46 of Follitropin subunit beta
Cysteine 100 of Follitropin subunit beta
1fl7 B 20 B 104
A redox-regulated disulphide may form within Follitropin subunit beta between cysteines 38 and 122 (20 and 104 respectively in this structure).
Details
Redox score ?
85
PDB code
1fl7
Structure name
human follicle stimulating hormone
Structure deposition date
2000-08-11
Thiol separation (Å)
2
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01225
Residue number A
38
Residue number B
122
Peptide name
Follitropin subunit beta
Ligandability
Cysteine 38 of Follitropin subunit beta
Cysteine 122 of Follitropin subunit beta
4ay9 E 3 E 51
A redox-regulated disulphide may form within Follitropin subunit beta between cysteines 21 and 69 (3 and 51 respectively in this structure).
Details
Redox score ?
83
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 ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01225
Residue number A
21
Residue number B
69
Peptide name
Follitropin subunit beta
Ligandability
Cysteine 21 of Follitropin subunit beta
Cysteine 69 of Follitropin subunit beta
4mqw H 87 H 94
A redox-regulated disulphide may form within Follitropin subunit beta between cysteines 105 and 112 (87 and 94 respectively in this structure).
Details
Redox score ?
81
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 ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01225
Residue number A
105
Residue number B
112
Peptide name
Follitropin subunit beta
Ligandability
Cysteine 105 of Follitropin subunit beta
Cysteine 112 of Follitropin subunit beta
4mqw B 32 B 84
A redox-regulated disulphide may form within Follitropin subunit beta between cysteines 50 and 102 (32 and 84 respectively in this structure).
Details
Redox score ?
81
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 ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01225
Residue number A
50
Residue number B
102
Peptide name
Follitropin subunit beta
Ligandability
Cysteine 50 of Follitropin subunit beta
Cysteine 102 of Follitropin subunit beta
1fl7 B 3 B 84
A redox-regulated disulphide may form within Follitropin subunit beta between cysteines 21 and 102 (3 and 84 respectively in this structure).
Details
Redox score ?
75
PDB code
1fl7
Structure name
human follicle stimulating hormone
Structure deposition date
2000-08-11
Thiol separation (Å)
5
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01225
Residue number A
21
Residue number B
102
Peptide name
Follitropin subunit beta
Ligandability
Cysteine 21 of Follitropin subunit beta
Cysteine 102 of Follitropin subunit beta
1fl7 B 3 B 82
A redox-regulated disulphide may form within Follitropin subunit beta between cysteines 21 and 100 (3 and 82 respectively in this structure).
Details
Redox score ?
73
PDB code
1fl7
Structure name
human follicle stimulating hormone
Structure deposition date
2000-08-11
Thiol separation (Å)
5
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01225
Residue number A
21
Residue number B
100
Peptide name
Follitropin subunit beta
Ligandability
Cysteine 21 of Follitropin subunit beta
Cysteine 100 of Follitropin subunit beta
1fl7 D 3 D 28
A redox-regulated disulphide may form within Follitropin subunit beta between cysteines 21 and 46 (3 and 28 respectively in this structure).
Details
Redox score ?
67
PDB code
1fl7
Structure name
human follicle stimulating hormone
Structure deposition date
2000-08-11
Thiol separation (Å)
6
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01225
Residue number A
21
Residue number B
46
Peptide name
Follitropin subunit beta
Ligandability
Cysteine 21 of Follitropin subunit beta
Cysteine 46 of Follitropin subunit beta
4mqw B 3 B 32
A redox-regulated disulphide may form within Follitropin subunit beta between cysteines 21 and 50 (3 and 32 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 ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01225
Residue number A
21
Residue number B
50
Peptide name
Follitropin subunit beta
Ligandability
Cysteine 21 of Follitropin subunit beta
Cysteine 50 of Follitropin subunit beta
4mqw E 51 E 82
A redox-regulated disulphide may form within Follitropin subunit beta between cysteines 69 and 100 (51 and 82 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 ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01225
Residue number A
69
Residue number B
100
Peptide name
Follitropin subunit beta
Ligandability
Cysteine 69 of Follitropin subunit beta
Cysteine 100 of Follitropin subunit beta
4ay9 E 32 E 51
A redox-regulated disulphide may form within Follitropin subunit beta between cysteines 50 and 69 (32 and 51 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)
5
Half-sphere exposure sum ?
84
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01225
Residue number A
50
Residue number B
69
Peptide name
Follitropin subunit beta
Ligandability
Cysteine 50 of Follitropin subunit beta
Cysteine 69 of Follitropin subunit beta
1fl7 B 51 B 84
A redox-regulated disulphide may form within Follitropin subunit beta between cysteines 69 and 102 (51 and 84 respectively in this structure).
Details
Redox score ?
60
PDB code
1fl7
Structure name
human follicle stimulating hormone
Structure deposition date
2000-08-11
Thiol separation (Å)
6
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01225
Residue number A
69
Residue number B
102
Peptide name
Follitropin subunit beta
Ligandability
Cysteine 69 of Follitropin subunit beta
Cysteine 102 of Follitropin subunit beta
1fl7 D 28 D 51
A redox-regulated disulphide may form within Follitropin subunit beta between cysteines 46 and 69 (28 and 51 respectively in this structure).
Details
Redox score ?
60
PDB code
1fl7
Structure name
human follicle stimulating hormone
Structure deposition date
2000-08-11
Thiol separation (Å)
5
Half-sphere exposure sum ?
83
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01225
Residue number A
46
Residue number B
69
Peptide name
Follitropin subunit beta
Ligandability
Cysteine 46 of Follitropin subunit beta
Cysteine 69 of Follitropin subunit beta
4mqw B 82 B 84
A redox-regulated disulphide may form within Follitropin subunit beta between cysteines 100 and 102 (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 ?
43
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 ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01225
Residue number A
100
Residue number B
102
Peptide name
Follitropin subunit beta
Ligandability
Cysteine 100 of Follitropin subunit beta
Cysteine 102 of Follitropin subunit beta
4mqw E 32 E 82
A redox-regulated disulphide may form within Follitropin subunit beta between cysteines 50 and 100 (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 ?
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 ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01225
Residue number A
50
Residue number B
100
Peptide name
Follitropin subunit beta
Ligandability
Cysteine 50 of Follitropin subunit beta
Cysteine 100 of Follitropin subunit beta
1fl7 D 28 D 84
A redox-regulated disulphide may form within Follitropin subunit beta between cysteines 46 and 102 (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 ?
38
PDB code
1fl7
Structure name
human follicle stimulating hormone
Structure deposition date
2000-08-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01225
Residue number A
46
Residue number B
102
Peptide name
Follitropin subunit beta
Ligandability
Cysteine 46 of Follitropin subunit beta
Cysteine 102 of Follitropin subunit beta
4mqw B 28 B 32
A redox-regulated disulphide may form within Follitropin subunit beta between cysteines 46 and 50 (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 ?
36
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 ?
83
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01225
Residue number A
46
Residue number B
50
Peptide name
Follitropin subunit beta
Ligandability
Cysteine 46 of Follitropin subunit beta
Cysteine 50 of Follitropin subunit beta
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