Anti-Muellerian hormone type-2 receptor
Intramolecular
Cysteine 60 and cysteine 87
Cysteine 92 and cysteine 109
Cysteine 55 and cysteine 79
Cysteine 24 and cysteine 61
Cysteine 111 and cysteine 116
Cysteine 24 and cysteine 55
Cysteine 24 and cysteine 79
Cysteine 61 and cysteine 116
Cysteine 92 and cysteine 111
Cysteine 55 and cysteine 61
More...Cysteine 109 and cysteine 111
Cysteine 24 and cysteine 116
Cysteine 92 and cysteine 116
Cysteine 61 and cysteine 111
Cysteine 61 and cysteine 79
Cysteine 109 and cysteine 116
Cysteine 60 and cysteine 111
Cysteine 60 and cysteine 116
Cysteine 24 and cysteine 60
Cysteine 60 and cysteine 61
Cysteine 24 and cysteine 111
Cysteine 87 and cysteine 111
Cysteine 87 and cysteine 116
Cysteine 55 and cysteine 60
Cysteine 24 and cysteine 87
Cysteine 61 and cysteine 87
Cysteine 55 and cysteine 87
Cysteine 55 and cysteine 116
Cysteine 60 and cysteine 109
Cysteine 87 and cysteine 109
Cysteine 60 and cysteine 79
Cysteine 61 and cysteine 92
Cysteine 61 and cysteine 109
Cysteine 79 and cysteine 116
7l0j B 60 B 87
A redox-regulated disulphide may form within Anti-Muellerian hormone type-2 receptor between cysteines 60 and 87.
Details
Redox score ?
82
PDB code
7l0j
Structure name
structure of amh bound to amhr2-ecd
Structure deposition date
2020-12-11
Thiol separation (Å)
2
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16671
Residue number A
60
Residue number B
87
Peptide name
Anti-Muellerian hormone type-2 receptor
Ligandability
Cysteine 60 of Anti-Muellerian hormone type-2 receptor
Cysteine 87 of Anti-Muellerian hormone type-2 receptor
7l0j B 92 B 109
A redox-regulated disulphide may form within Anti-Muellerian hormone type-2 receptor between cysteines 92 and 109.
Details
Redox score ?
81
PDB code
7l0j
Structure name
structure of amh bound to amhr2-ecd
Structure deposition date
2020-12-11
Thiol separation (Å)
2
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16671
Residue number A
92
Residue number B
109
Peptide name
Anti-Muellerian hormone type-2 receptor
Ligandability
Cysteine 92 of Anti-Muellerian hormone type-2 receptor
Cysteine 109 of Anti-Muellerian hormone type-2 receptor
7l0j B 55 B 79
A redox-regulated disulphide may form within Anti-Muellerian hormone type-2 receptor between cysteines 55 and 79.
Details
Redox score ?
80
PDB code
7l0j
Structure name
structure of amh bound to amhr2-ecd
Structure deposition date
2020-12-11
Thiol separation (Å)
2
Half-sphere exposure sum ?
87
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16671
Residue number A
55
Residue number B
79
Peptide name
Anti-Muellerian hormone type-2 receptor
Ligandability
Cysteine 55 of Anti-Muellerian hormone type-2 receptor
Cysteine 79 of Anti-Muellerian hormone type-2 receptor
7l0j B 24 B 61
A redox-regulated disulphide may form within Anti-Muellerian hormone type-2 receptor between cysteines 24 and 61.
Details
Redox score ?
79
PDB code
7l0j
Structure name
structure of amh bound to amhr2-ecd
Structure deposition date
2020-12-11
Thiol separation (Å)
2
Half-sphere exposure sum ?
98
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16671
Residue number A
24
Residue number B
61
Peptide name
Anti-Muellerian hormone type-2 receptor
Ligandability
Cysteine 24 of Anti-Muellerian hormone type-2 receptor
Cysteine 61 of Anti-Muellerian hormone type-2 receptor
7l0j B 111 B 116
A redox-regulated disulphide may form within Anti-Muellerian hormone type-2 receptor between cysteines 111 and 116.
Details
Redox score ?
78
PDB code
7l0j
Structure name
structure of amh bound to amhr2-ecd
Structure deposition date
2020-12-11
Thiol separation (Å)
2
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16671
Residue number A
111
Residue number B
116
Peptide name
Anti-Muellerian hormone type-2 receptor
Ligandability
Cysteine 111 of Anti-Muellerian hormone type-2 receptor
Cysteine 116 of Anti-Muellerian hormone type-2 receptor
7l0j B 24 B 55
A redox-regulated disulphide may form within Anti-Muellerian hormone type-2 receptor between cysteines 24 and 55.
Details
Redox score ?
76
PDB code
7l0j
Structure name
structure of amh bound to amhr2-ecd
Structure deposition date
2020-12-11
Thiol separation (Å)
3
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16671
Residue number A
24
Residue number B
55
Peptide name
Anti-Muellerian hormone type-2 receptor
Ligandability
Cysteine 24 of Anti-Muellerian hormone type-2 receptor
Cysteine 55 of Anti-Muellerian hormone type-2 receptor
7l0j B 24 B 79
A redox-regulated disulphide may form within Anti-Muellerian hormone type-2 receptor between cysteines 24 and 79.
Details
Redox score ?
69
PDB code
7l0j
Structure name
structure of amh bound to amhr2-ecd
Structure deposition date
2020-12-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
96
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16671
Residue number A
24
Residue number B
79
Peptide name
Anti-Muellerian hormone type-2 receptor
Ligandability
Cysteine 24 of Anti-Muellerian hormone type-2 receptor
Cysteine 79 of Anti-Muellerian hormone type-2 receptor
7l0j B 61 B 116
A redox-regulated disulphide may form within Anti-Muellerian hormone type-2 receptor between cysteines 61 and 116.
Details
Redox score ?
65
PDB code
7l0j
Structure name
structure of amh bound to amhr2-ecd
Structure deposition date
2020-12-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
87
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16671
Residue number A
61
Residue number B
116
Peptide name
Anti-Muellerian hormone type-2 receptor
Ligandability
Cysteine 61 of Anti-Muellerian hormone type-2 receptor
Cysteine 116 of Anti-Muellerian hormone type-2 receptor
7l0j B 92 B 111
A redox-regulated disulphide may form within Anti-Muellerian hormone type-2 receptor between cysteines 92 and 111.
Details
Redox score ?
63
PDB code
7l0j
Structure name
structure of amh bound to amhr2-ecd
Structure deposition date
2020-12-11
Thiol separation (Å)
5
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16671
Residue number A
92
Residue number B
111
Peptide name
Anti-Muellerian hormone type-2 receptor
Ligandability
Cysteine 92 of Anti-Muellerian hormone type-2 receptor
Cysteine 111 of Anti-Muellerian hormone type-2 receptor
7l0j B 55 B 61
A redox-regulated disulphide may form within Anti-Muellerian hormone type-2 receptor between cysteines 55 and 61.
Details
Redox score ?
62
PDB code
7l0j
Structure name
structure of amh bound to amhr2-ecd
Structure deposition date
2020-12-11
Thiol separation (Å)
5
Half-sphere exposure sum ?
89
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16671
Residue number A
55
Residue number B
61
Peptide name
Anti-Muellerian hormone type-2 receptor
Ligandability
Cysteine 55 of Anti-Muellerian hormone type-2 receptor
Cysteine 61 of Anti-Muellerian hormone type-2 receptor
7l0j B 109 B 111
A redox-regulated disulphide may form within Anti-Muellerian hormone type-2 receptor between cysteines 109 and 111.
Details
Redox score ?
61
PDB code
7l0j
Structure name
structure of amh bound to amhr2-ecd
Structure deposition date
2020-12-11
Thiol separation (Å)
5
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16671
Residue number A
109
Residue number B
111
Peptide name
Anti-Muellerian hormone type-2 receptor
Ligandability
Cysteine 109 of Anti-Muellerian hormone type-2 receptor
Cysteine 111 of Anti-Muellerian hormone type-2 receptor
7l0j B 24 B 116
A redox-regulated disulphide may form within Anti-Muellerian hormone type-2 receptor between cysteines 24 and 116. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
57
PDB code
7l0j
Structure name
structure of amh bound to amhr2-ecd
Structure deposition date
2020-12-11
Thiol separation (Å)
6
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16671
Residue number A
24
Residue number B
116
Peptide name
Anti-Muellerian hormone type-2 receptor
Ligandability
Cysteine 24 of Anti-Muellerian hormone type-2 receptor
Cysteine 116 of Anti-Muellerian hormone type-2 receptor
7l0j B 92 B 116
A redox-regulated disulphide may form within Anti-Muellerian hormone type-2 receptor between cysteines 92 and 116. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
55
PDB code
7l0j
Structure name
structure of amh bound to amhr2-ecd
Structure deposition date
2020-12-11
Thiol separation (Å)
7
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16671
Residue number A
92
Residue number B
116
Peptide name
Anti-Muellerian hormone type-2 receptor
Ligandability
Cysteine 92 of Anti-Muellerian hormone type-2 receptor
Cysteine 116 of Anti-Muellerian hormone type-2 receptor
7l0j B 61 B 111
A redox-regulated disulphide may form within Anti-Muellerian hormone type-2 receptor between cysteines 61 and 111. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
55
PDB code
7l0j
Structure name
structure of amh bound to amhr2-ecd
Structure deposition date
2020-12-11
Thiol separation (Å)
6
Half-sphere exposure sum ?
92
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16671
Residue number A
61
Residue number B
111
Peptide name
Anti-Muellerian hormone type-2 receptor
Ligandability
Cysteine 61 of Anti-Muellerian hormone type-2 receptor
Cysteine 111 of Anti-Muellerian hormone type-2 receptor
7l0j B 61 B 79
A redox-regulated disulphide may form within Anti-Muellerian hormone type-2 receptor between cysteines 61 and 79. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
53
PDB code
7l0j
Structure name
structure of amh bound to amhr2-ecd
Structure deposition date
2020-12-11
Thiol separation (Å)
6
Half-sphere exposure sum ?
104
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16671
Residue number A
61
Residue number B
79
Peptide name
Anti-Muellerian hormone type-2 receptor
Ligandability
Cysteine 61 of Anti-Muellerian hormone type-2 receptor
Cysteine 79 of Anti-Muellerian hormone type-2 receptor
7l0j B 109 B 116
A redox-regulated disulphide may form within Anti-Muellerian hormone type-2 receptor between cysteines 109 and 116. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
52
PDB code
7l0j
Structure name
structure of amh bound to amhr2-ecd
Structure deposition date
2020-12-11
Thiol separation (Å)
7
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16671
Residue number A
109
Residue number B
116
Peptide name
Anti-Muellerian hormone type-2 receptor
Ligandability
Cysteine 109 of Anti-Muellerian hormone type-2 receptor
Cysteine 116 of Anti-Muellerian hormone type-2 receptor
7l0j B 60 B 111
A redox-regulated disulphide may form within Anti-Muellerian hormone type-2 receptor between cysteines 60 and 111. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
7l0j
Structure name
structure of amh bound to amhr2-ecd
Structure deposition date
2020-12-11
Thiol separation (Å)
6
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16671
Residue number A
60
Residue number B
111
Peptide name
Anti-Muellerian hormone type-2 receptor
Ligandability
Cysteine 60 of Anti-Muellerian hormone type-2 receptor
Cysteine 111 of Anti-Muellerian hormone type-2 receptor
7l0j B 60 B 116
A redox-regulated disulphide may form within Anti-Muellerian hormone type-2 receptor between cysteines 60 and 116. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
7l0j
Structure name
structure of amh bound to amhr2-ecd
Structure deposition date
2020-12-11
Thiol separation (Å)
7
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16671
Residue number A
60
Residue number B
116
Peptide name
Anti-Muellerian hormone type-2 receptor
Ligandability
Cysteine 60 of Anti-Muellerian hormone type-2 receptor
Cysteine 116 of Anti-Muellerian hormone type-2 receptor
7l0j B 24 B 60
A redox-regulated disulphide may form within Anti-Muellerian hormone type-2 receptor between cysteines 24 and 60. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
7l0j
Structure name
structure of amh bound to amhr2-ecd
Structure deposition date
2020-12-11
Thiol separation (Å)
7
Half-sphere exposure sum ?
88
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16671
Residue number A
24
Residue number B
60
Peptide name
Anti-Muellerian hormone type-2 receptor
Ligandability
Cysteine 24 of Anti-Muellerian hormone type-2 receptor
Cysteine 60 of Anti-Muellerian hormone type-2 receptor
7l0j B 60 B 61
A redox-regulated disulphide may form within Anti-Muellerian hormone type-2 receptor between cysteines 60 and 61. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
7l0j
Structure name
structure of amh bound to amhr2-ecd
Structure deposition date
2020-12-11
Thiol separation (Å)
7
Half-sphere exposure sum ?
96
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16671
Residue number A
60
Residue number B
61
Peptide name
Anti-Muellerian hormone type-2 receptor
Ligandability
Cysteine 60 of Anti-Muellerian hormone type-2 receptor
Cysteine 61 of Anti-Muellerian hormone type-2 receptor
7l0j B 24 B 111
A redox-regulated disulphide may form within Anti-Muellerian hormone type-2 receptor between cysteines 24 and 111. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
7l0j
Structure name
structure of amh bound to amhr2-ecd
Structure deposition date
2020-12-11
Thiol separation (Å)
7
Half-sphere exposure sum ?
84
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16671
Residue number A
24
Residue number B
111
Peptide name
Anti-Muellerian hormone type-2 receptor
Ligandability
Cysteine 24 of Anti-Muellerian hormone type-2 receptor
Cysteine 111 of Anti-Muellerian hormone type-2 receptor
7l0j B 87 B 111
A redox-regulated disulphide may form within Anti-Muellerian hormone type-2 receptor between cysteines 87 and 111. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
7l0j
Structure name
structure of amh bound to amhr2-ecd
Structure deposition date
2020-12-11
Thiol separation (Å)
8
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16671
Residue number A
87
Residue number B
111
Peptide name
Anti-Muellerian hormone type-2 receptor
Ligandability
Cysteine 87 of Anti-Muellerian hormone type-2 receptor
Cysteine 111 of Anti-Muellerian hormone type-2 receptor
7l0j B 87 B 116
A redox-regulated disulphide may form within Anti-Muellerian hormone type-2 receptor between cysteines 87 and 116. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
7l0j
Structure name
structure of amh bound to amhr2-ecd
Structure deposition date
2020-12-11
Thiol separation (Å)
8
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16671
Residue number A
87
Residue number B
116
Peptide name
Anti-Muellerian hormone type-2 receptor
Ligandability
Cysteine 87 of Anti-Muellerian hormone type-2 receptor
Cysteine 116 of Anti-Muellerian hormone type-2 receptor
7l0j B 55 B 60
A redox-regulated disulphide may form within Anti-Muellerian hormone type-2 receptor between cysteines 55 and 60. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
7l0j
Structure name
structure of amh bound to amhr2-ecd
Structure deposition date
2020-12-11
Thiol separation (Å)
8
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16671
Residue number A
55
Residue number B
60
Peptide name
Anti-Muellerian hormone type-2 receptor
Ligandability
Cysteine 55 of Anti-Muellerian hormone type-2 receptor
Cysteine 60 of Anti-Muellerian hormone type-2 receptor
7l0j B 24 B 87
A redox-regulated disulphide may form within Anti-Muellerian hormone type-2 receptor between cysteines 24 and 87. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
7l0j
Structure name
structure of amh bound to amhr2-ecd
Structure deposition date
2020-12-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16671
Residue number A
24
Residue number B
87
Peptide name
Anti-Muellerian hormone type-2 receptor
Ligandability
Cysteine 24 of Anti-Muellerian hormone type-2 receptor
Cysteine 87 of Anti-Muellerian hormone type-2 receptor
7l0j B 61 B 87
A redox-regulated disulphide may form within Anti-Muellerian hormone type-2 receptor between cysteines 61 and 87. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
7l0j
Structure name
structure of amh bound to amhr2-ecd
Structure deposition date
2020-12-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
89
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16671
Residue number A
61
Residue number B
87
Peptide name
Anti-Muellerian hormone type-2 receptor
Ligandability
Cysteine 61 of Anti-Muellerian hormone type-2 receptor
Cysteine 87 of Anti-Muellerian hormone type-2 receptor
7l0j B 55 B 87
A redox-regulated disulphide may form within Anti-Muellerian hormone type-2 receptor between cysteines 55 and 87. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
7l0j
Structure name
structure of amh bound to amhr2-ecd
Structure deposition date
2020-12-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16671
Residue number A
55
Residue number B
87
Peptide name
Anti-Muellerian hormone type-2 receptor
Ligandability
Cysteine 55 of Anti-Muellerian hormone type-2 receptor
Cysteine 87 of Anti-Muellerian hormone type-2 receptor
7l0j B 55 B 116
A redox-regulated disulphide may form within Anti-Muellerian hormone type-2 receptor between cysteines 55 and 116. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
7l0j
Structure name
structure of amh bound to amhr2-ecd
Structure deposition date
2020-12-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16671
Residue number A
55
Residue number B
116
Peptide name
Anti-Muellerian hormone type-2 receptor
Ligandability
Cysteine 55 of Anti-Muellerian hormone type-2 receptor
Cysteine 116 of Anti-Muellerian hormone type-2 receptor
7l0j B 60 B 109
A redox-regulated disulphide may form within Anti-Muellerian hormone type-2 receptor between cysteines 60 and 109. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
7l0j
Structure name
structure of amh bound to amhr2-ecd
Structure deposition date
2020-12-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
86
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16671
Residue number A
60
Residue number B
109
Peptide name
Anti-Muellerian hormone type-2 receptor
Ligandability
Cysteine 60 of Anti-Muellerian hormone type-2 receptor
Cysteine 109 of Anti-Muellerian hormone type-2 receptor
7l0j B 87 B 109
A redox-regulated disulphide may form within Anti-Muellerian hormone type-2 receptor between cysteines 87 and 109. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
7l0j
Structure name
structure of amh bound to amhr2-ecd
Structure deposition date
2020-12-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16671
Residue number A
87
Residue number B
109
Peptide name
Anti-Muellerian hormone type-2 receptor
Ligandability
Cysteine 87 of Anti-Muellerian hormone type-2 receptor
Cysteine 109 of Anti-Muellerian hormone type-2 receptor
7l0j B 60 B 79
A redox-regulated disulphide may form within Anti-Muellerian hormone type-2 receptor between cysteines 60 and 79. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
36
PDB code
7l0j
Structure name
structure of amh bound to amhr2-ecd
Structure deposition date
2020-12-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
94
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16671
Residue number A
60
Residue number B
79
Peptide name
Anti-Muellerian hormone type-2 receptor
Ligandability
Cysteine 60 of Anti-Muellerian hormone type-2 receptor
Cysteine 79 of Anti-Muellerian hormone type-2 receptor
7l0j B 61 B 92
A redox-regulated disulphide may form within Anti-Muellerian hormone type-2 receptor between cysteines 61 and 92. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
36
PDB code
7l0j
Structure name
structure of amh bound to amhr2-ecd
Structure deposition date
2020-12-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
88
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16671
Residue number A
61
Residue number B
92
Peptide name
Anti-Muellerian hormone type-2 receptor
Ligandability
Cysteine 61 of Anti-Muellerian hormone type-2 receptor
Cysteine 92 of Anti-Muellerian hormone type-2 receptor
7l0j B 61 B 109
A redox-regulated disulphide may form within Anti-Muellerian hormone type-2 receptor between cysteines 61 and 109. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
35
PDB code
7l0j
Structure name
structure of amh bound to amhr2-ecd
Structure deposition date
2020-12-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
96
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16671
Residue number A
61
Residue number B
109
Peptide name
Anti-Muellerian hormone type-2 receptor
Ligandability
Cysteine 61 of Anti-Muellerian hormone type-2 receptor
Cysteine 109 of Anti-Muellerian hormone type-2 receptor
7l0j B 79 B 116
A redox-regulated disulphide may form within Anti-Muellerian hormone type-2 receptor between cysteines 79 and 116. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
33
PDB code
7l0j
Structure name
structure of amh bound to amhr2-ecd
Structure deposition date
2020-12-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
85
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16671
Residue number A
79
Residue number B
116
Peptide name
Anti-Muellerian hormone type-2 receptor
Ligandability
Cysteine 79 of Anti-Muellerian hormone type-2 receptor
Cysteine 116 of Anti-Muellerian hormone type-2 receptor
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