Glycoprotein hormones alpha chain
Intermolecular
Cysteine 31 and cysteine 102 of Follitropin subunit beta
Cysteine 31 and cysteine 50 of Follitropin subunit beta
Cysteine 31 and cysteine 51 of Thyrotropin subunit beta
Cysteine 31 and cysteine 22 of Thyrotropin subunit beta
Cysteine 111 and cysteine 113 of Choriogonadotropin subunit beta 3
Cysteine 31 and cysteine 21 of Follitropin subunit beta
Cysteine 111 and cysteine 120 of Choriogonadotropin subunit beta 3
Cysteine 31 and cysteine 58 of Choriogonadotropin subunit beta 3
Cysteine 31 and cysteine 105 of Thyrotropin subunit beta
Cysteine 55 and cysteine 50 of Follitropin subunit beta
More...Cysteine 31 and cysteine 110 of Choriogonadotropin subunit beta 3
Cysteine 55 and cysteine 102 of Follitropin subunit beta
Cysteine 31 and cysteine 72 of Thyrotropin subunit beta
Cysteine 55 and cysteine 58 of Choriogonadotropin subunit beta 3
Cysteine 111 and cysteine 105 of Follitropin subunit beta
Cysteine 55 and cysteine 22 of Thyrotropin subunit beta
Cysteine 111 and cysteine 108 of Thyrotropin subunit beta
Intramolecular
Cysteine 52 and cysteine 106
Cysteine 83 and cysteine 111
Cysteine 34 and cysteine 84
Cysteine 31 and cysteine 55
Cysteine 56 and cysteine 108
Cysteine 34 and cysteine 106
Cysteine 34 and cysteine 56
Cysteine 34 and cysteine 108
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 55 and cysteine 83
Cysteine 56 and cysteine 83
Cysteine 56 and cysteine 111
Cysteine 83 and cysteine 106
Cysteine 55 and cysteine 56
Cysteine 31 and cysteine 111
Cysteine 106 and cysteine 108
Cysteine 34 and cysteine 55
Cysteine 31 and cysteine 106
Cysteine 31 and cysteine 56
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
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
7xw5 X 7 Y 51
A redox-regulated disulphide may form between cysteine 31 of Glycoprotein hormones alpha chain and cysteine 51 of Thyrotropin 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 ?
54
PDB code
7xw5
Structure name
tshr-thyroid stimulating hormone-gs-ml109 complex
Structure deposition date
2022-05-26
Thiol separation (Å)
7
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide A name
Glycoprotein hormones alpha chain
Peptide B name
Thyrotropin subunit beta
Peptide A accession
P01215
Peptide B accession
P01222
Peptide A residue number
31
Peptide B residue number
51
Ligandability
Cysteine 31 of Glycoprotein hormones alpha chain
Cysteine 51 of Thyrotropin subunit beta
7xw5 X 7 Y 22
A redox-regulated disulphide may form between cysteine 31 of Glycoprotein hormones alpha chain and cysteine 22 of Thyrotropin subunit beta (7 and 22 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
7xw5
Structure name
tshr-thyroid stimulating hormone-gs-ml109 complex
Structure deposition date
2022-05-26
Thiol separation (Å)
8
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide A name
Glycoprotein hormones alpha chain
Peptide B name
Thyrotropin subunit beta
Peptide A accession
P01215
Peptide B accession
P01222
Peptide A residue number
31
Peptide B residue number
22
Ligandability
Cysteine 31 of Glycoprotein hormones alpha chain
Cysteine 22 of Thyrotropin subunit beta
7fig X 87 Y 93
A redox-regulated disulphide may form between cysteine 111 of Glycoprotein hormones alpha chain and cysteine 113 of Choriogonadotropin subunit beta 3 (87 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 ?
52
PDB code
7fig
Structure name
luteinizing hormone/choriogonadotropin receptor(s277i)-chorionic gonadotropin-gs complex
Structure deposition date
2021-07-31
Thiol separation (Å)
8
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide A name
Glycoprotein hormones alpha chain
Peptide B name
Choriogonadotropin subunit beta 3
Peptide A accession
P01215
Peptide B accession
P0DN86
Peptide A residue number
111
Peptide B residue number
113
Ligandability
Cysteine 111 of Glycoprotein hormones alpha chain
Cysteine 113 of Choriogonadotropin subunit beta 3
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
7fih X 87 Y 100
A redox-regulated disulphide may form between cysteine 111 of Glycoprotein hormones alpha chain and cysteine 120 of Choriogonadotropin subunit beta 3 (87 and 100 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
7fih
Structure name
luteinizing hormone/choriogonadotropin receptor(s277i)-chorionic gonadotropin-gs-org43553 complex
Structure deposition date
2021-07-31
Thiol separation (Å)
8
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide A name
Glycoprotein hormones alpha chain
Peptide B name
Choriogonadotropin subunit beta 3
Peptide A accession
P01215
Peptide B accession
P0DN86
Peptide A residue number
111
Peptide B residue number
120
Ligandability
Cysteine 111 of Glycoprotein hormones alpha chain
Cysteine 120 of Choriogonadotropin subunit beta 3
7fig X 7 Y 38
A redox-regulated disulphide may form between cysteine 31 of Glycoprotein hormones alpha chain and cysteine 58 of Choriogonadotropin subunit beta 3 (7 and 38 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
7fig
Structure name
luteinizing hormone/choriogonadotropin receptor(s277i)-chorionic gonadotropin-gs complex
Structure deposition date
2021-07-31
Thiol separation (Å)
8
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide A name
Glycoprotein hormones alpha chain
Peptide B name
Choriogonadotropin subunit beta 3
Peptide A accession
P01215
Peptide B accession
P0DN86
Peptide A residue number
31
Peptide B residue number
58
Ligandability
Cysteine 31 of Glycoprotein hormones alpha chain
Cysteine 58 of Choriogonadotropin subunit beta 3
7xw5 X 7 Y 105
A redox-regulated disulphide may form between cysteine 31 of Glycoprotein hormones alpha chain and cysteine 105 of Thyrotropin subunit beta (7 and 105 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
7xw5
Structure name
tshr-thyroid stimulating hormone-gs-ml109 complex
Structure deposition date
2022-05-26
Thiol separation (Å)
9
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide A name
Glycoprotein hormones alpha chain
Peptide B name
Thyrotropin subunit beta
Peptide A accession
P01215
Peptide B accession
P01222
Peptide A residue number
31
Peptide B residue number
105
Ligandability
Cysteine 31 of Glycoprotein hormones alpha chain
Cysteine 105 of Thyrotropin 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
7fih X 7 Y 90
A redox-regulated disulphide may form between cysteine 31 of Glycoprotein hormones alpha chain and cysteine 110 of Choriogonadotropin subunit beta 3 (7 and 90 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
7fih
Structure name
luteinizing hormone/choriogonadotropin receptor(s277i)-chorionic gonadotropin-gs-org43553 complex
Structure deposition date
2021-07-31
Thiol separation (Å)
9
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide A name
Glycoprotein hormones alpha chain
Peptide B name
Choriogonadotropin subunit beta 3
Peptide A accession
P01215
Peptide B accession
P0DN86
Peptide A residue number
31
Peptide B residue number
110
Ligandability
Cysteine 31 of Glycoprotein hormones alpha chain
Cysteine 110 of Choriogonadotropin subunit beta 3
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
7xw5 X 7 Y 72
A redox-regulated disulphide may form between cysteine 31 of Glycoprotein hormones alpha chain and cysteine 72 of Thyrotropin subunit beta (7 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 ?
46
PDB code
7xw5
Structure name
tshr-thyroid stimulating hormone-gs-ml109 complex
Structure deposition date
2022-05-26
Thiol separation (Å)
9
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide A name
Glycoprotein hormones alpha chain
Peptide B name
Thyrotropin subunit beta
Peptide A accession
P01215
Peptide B accession
P01222
Peptide A residue number
31
Peptide B residue number
72
Ligandability
Cysteine 31 of Glycoprotein hormones alpha chain
Cysteine 72 of Thyrotropin subunit beta
7fih X 31 Y 38
A redox-regulated disulphide may form between cysteine 55 of Glycoprotein hormones alpha chain and cysteine 58 of Choriogonadotropin subunit beta 3 (31 and 38 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
7fih
Structure name
luteinizing hormone/choriogonadotropin receptor(s277i)-chorionic gonadotropin-gs-org43553 complex
Structure deposition date
2021-07-31
Thiol separation (Å)
8
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide A name
Glycoprotein hormones alpha chain
Peptide B name
Choriogonadotropin subunit beta 3
Peptide A accession
P01215
Peptide B accession
P0DN86
Peptide A residue number
55
Peptide B residue number
58
Ligandability
Cysteine 55 of Glycoprotein hormones alpha chain
Cysteine 58 of Choriogonadotropin subunit beta 3
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
7xw5 X 31 Y 22
A redox-regulated disulphide may form between cysteine 55 of Glycoprotein hormones alpha chain and cysteine 22 of Thyrotropin subunit beta (31 and 22 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
7xw5
Structure name
tshr-thyroid stimulating hormone-gs-ml109 complex
Structure deposition date
2022-05-26
Thiol separation (Å)
9
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide A name
Glycoprotein hormones alpha chain
Peptide B name
Thyrotropin subunit beta
Peptide A accession
P01215
Peptide B accession
P01222
Peptide A residue number
55
Peptide B residue number
22
Ligandability
Cysteine 55 of Glycoprotein hormones alpha chain
Cysteine 22 of Thyrotropin subunit beta
7utz A 87 B 88
A redox-regulated disulphide may form between cysteine 111 of Glycoprotein hormones alpha chain and cysteine 108 of Thyrotropin subunit beta (87 and 88 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
7utz
Structure name
human thyrotropin analog tr1402 bound to human thyrotropin receptor in complex with minigs399 (composite structure)
Structure deposition date
2022-04-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide A name
Glycoprotein hormones alpha chain
Peptide B name
Thyrotropin subunit beta
Peptide A accession
P01215
Peptide B accession
P01222
Peptide A residue number
111
Peptide B residue number
108
Ligandability
Cysteine 111 of Glycoprotein hormones alpha chain
Cysteine 108 of Thyrotropin subunit beta
1qfw 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
1qfw
Structure name
ternary complex of human chorionic gonadotropin with fv anti alpha subunit and fv anti beta subunit
Structure deposition date
1999-04-15
Thiol separation (Å)
2
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01215
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
1qfw A 59 A 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 ?
85
PDB code
1qfw
Structure name
ternary complex of human chorionic gonadotropin with fv anti alpha subunit and fv anti beta subunit
Structure deposition date
1999-04-15
Thiol separation (Å)
2
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01215
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
1hcn 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
1hcn
Structure name
structure of human chorionic gonadotropin at 2
Structure deposition date
1994-07-01
Thiol separation (Å)
2
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01215
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
1hrp A 7 A 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 ?
83
PDB code
1hrp
Structure name
crystal structure of human chorionic gonadotropin
Structure deposition date
1994-08-15
Thiol separation (Å)
2
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01215
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
1fl7 C 32 C 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 ?
81
PDB code
1fl7
Structure name
human follicle stimulating hormone
Structure deposition date
2000-08-11
Thiol separation (Å)
2
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01215
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
1qfw 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
1qfw
Structure name
ternary complex of human chorionic gonadotropin with fv anti alpha subunit and fv anti beta subunit
Structure deposition date
1999-04-15
Thiol separation (Å)
5
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01215
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
1fl7 A 10 A 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 ?
72
PDB code
1fl7
Structure name
human follicle stimulating hormone
Structure deposition date
2000-08-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01215
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
1fl7 A 10 A 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 ?
70
PDB code
1fl7
Structure name
human follicle stimulating hormone
Structure deposition date
2000-08-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01215
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
1hcn A 60 A 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
1hcn
Structure name
structure of human chorionic gonadotropin at 2
Structure deposition date
1994-07-01
Thiol separation (Å)
5
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01215
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
1qfw 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
1qfw
Structure name
ternary complex of human chorionic gonadotropin with fv anti alpha subunit and fv anti beta subunit
Structure deposition date
1999-04-15
Thiol separation (Å)
5
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01215
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
1hrp A 32 A 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
1hrp
Structure name
crystal structure of human chorionic gonadotropin
Structure deposition date
1994-08-15
Thiol separation (Å)
5
Half-sphere exposure sum ?
83
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01215
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
1fl7 A 28 A 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
1fl7
Structure name
human follicle stimulating hormone
Structure deposition date
2000-08-11
Thiol separation (Å)
5
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01215
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
1hcn A 60 A 84
A redox-regulated disulphide may form within Glycoprotein hormones alpha chain between cysteines 84 and 108 (60 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 ?
58
PDB code
1hcn
Structure name
structure of human chorionic gonadotropin at 2
Structure deposition date
1994-07-01
Thiol separation (Å)
6
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01215
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
1dz7 A 31 A 59
A redox-regulated disulphide may form within Glycoprotein hormones alpha chain between cysteines 55 and 83 (31 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 ?
55
PDB code
1dz7
Structure name
solution structure of the a-subunit of human chorionic gonadotropin [modeled without carbohydrate residues]
Structure deposition date
2000-02-18
Thiol separation (Å)
7
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01215
Residue number A
55
Residue number B
83
Peptide name
Glycoprotein hormones alpha chain
Ligandability
Cysteine 55 of Glycoprotein hormones alpha chain
Cysteine 83 of Glycoprotein hormones alpha chain
1hrp 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 ?
54
PDB code
1hrp
Structure name
crystal structure of human chorionic gonadotropin
Structure deposition date
1994-08-15
Thiol separation (Å)
6
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01215
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
1qfw A 32 A 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 ?
49
PDB code
1qfw
Structure name
ternary complex of human chorionic gonadotropin with fv anti alpha subunit and fv anti beta subunit
Structure deposition date
1999-04-15
Thiol separation (Å)
8
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01215
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
1dz7 A 59 A 82
A redox-regulated disulphide may form within Glycoprotein hormones alpha chain between cysteines 83 and 106 (59 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 ?
48
PDB code
1dz7
Structure name
solution structure of the a-subunit of human chorionic gonadotropin [modeled without carbohydrate residues]
Structure deposition date
2000-02-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01215
Residue number A
83
Residue number B
106
Peptide name
Glycoprotein hormones alpha chain
Ligandability
Cysteine 83 of Glycoprotein hormones alpha chain
Cysteine 106 of Glycoprotein hormones alpha chain
1qfw 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 ?
47
PDB code
1qfw
Structure name
ternary complex of human chorionic gonadotropin with fv anti alpha subunit and fv anti beta subunit
Structure deposition date
1999-04-15
Thiol separation (Å)
7
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01215
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
1e9j A 7 A 87
A redox-regulated disulphide may form within Glycoprotein hormones alpha chain between cysteines 31 and 111 (7 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 ?
46
PDB code
1e9j
Structure name
solution structure of the a-subunit of human chorionic gonadotropin [including a single glcnac residue at asn52 and asn78]
Structure deposition date
2000-10-18
Thiol separation (Å)
10
Half-sphere exposure sum ?
34
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01215
Residue number A
31
Residue number B
111
Peptide name
Glycoprotein hormones alpha chain
Ligandability
Cysteine 31 of Glycoprotein hormones alpha chain
Cysteine 111 of Glycoprotein hormones alpha chain
1hrp 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 ?
45
PDB code
1hrp
Structure name
crystal structure of human chorionic gonadotropin
Structure deposition date
1994-08-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01215
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
1fl7 C 10 C 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
1fl7
Structure name
human follicle stimulating hormone
Structure deposition date
2000-08-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01215
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
1e9j A 7 A 82
A redox-regulated disulphide may form within Glycoprotein hormones alpha chain between cysteines 31 and 106 (7 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 ?
44
PDB code
1e9j
Structure name
solution structure of the a-subunit of human chorionic gonadotropin [including a single glcnac residue at asn52 and asn78]
Structure deposition date
2000-10-18
Thiol separation (Å)
10
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01215
Residue number A
31
Residue number B
106
Peptide name
Glycoprotein hormones alpha chain
Ligandability
Cysteine 31 of Glycoprotein hormones alpha chain
Cysteine 106 of Glycoprotein hormones alpha chain
1hcn A 7 A 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 ?
44
PDB code
1hcn
Structure name
structure of human chorionic gonadotropin at 2
Structure deposition date
1994-07-01
Thiol separation (Å)
9
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01215
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
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