Bone morphogenetic protein type II receptor
Intramolecular
Cysteine 25 and cysteine 49
Cysteine 64 and cysteine 81
Cysteine 34 and cysteine 31
Cysteine 59 and cysteine 82
Cysteine 34 and cysteine 25
Cysteine 83 and cysteine 88
Cysteine 64 and cysteine 83
Cysteine 31 and cysteine 88
Cysteine 25 and cysteine 31
Cysteine 34 and cysteine 49
More...Cysteine 64 and cysteine 88
Cysteine 31 and cysteine 83
Cysteine 34 and cysteine 88
Cysteine 81 and cysteine 83
Cysteine 34 and cysteine 83
Cysteine 64 and cysteine 82
Cysteine 59 and cysteine 64
Cysteine 59 and cysteine 83
Cysteine 31 and cysteine 49
Cysteine 31 and cysteine 64
Cysteine 81 and cysteine 88
Cysteine 81 and cysteine 82
Cysteine 82 and cysteine 83
Cysteine 59 and cysteine 88
Cysteine 59 and cysteine 81
Cysteine 34 and cysteine 64
Cysteine 25 and cysteine 88
Cysteine 31 and cysteine 59
Cysteine 34 and cysteine 59
Cysteine 82 and cysteine 88
Cysteine 31 and cysteine 81
Cysteine 31 and cysteine 82
2hlr A 60 A 84
A redox-regulated disulphide may form within Bone morphogenetic protein type II receptor between cysteines 25 and 49 (60 and 84 respectively in this structure).
Details
Redox score ?
85
PDB code
2hlr
Structure name
crystal structure of the extracellular domain of the type ii bmp receptor
Structure deposition date
2006-07-10
Thiol separation (Å)
2
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q91WY9
Residue number A
25
Residue number B
49
Peptide name
Bone morphogenetic protein type II receptor
Ligandability
Cysteine 25 of Bone morphogenetic protein type II receptor
Cysteine 49 of Bone morphogenetic protein type II receptor
2hlr A 99 A 116
A redox-regulated disulphide may form within Bone morphogenetic protein type II receptor between cysteines 64 and 81 (99 and 116 respectively in this structure).
Details
Redox score ?
84
PDB code
2hlr
Structure name
crystal structure of the extracellular domain of the type ii bmp receptor
Structure deposition date
2006-07-10
Thiol separation (Å)
2
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q91WY9
Residue number A
64
Residue number B
81
Peptide name
Bone morphogenetic protein type II receptor
Ligandability
Cysteine 64 of Bone morphogenetic protein type II receptor
Cysteine 81 of Bone morphogenetic protein type II receptor
2hlr A 34 A 66
A redox-regulated disulphide may form within Bone morphogenetic protein type II receptor between cysteines 34 and 31 (34 and 66 respectively in this structure).
Details
Redox score ?
82
PDB code
2hlr
Structure name
crystal structure of the extracellular domain of the type ii bmp receptor
Structure deposition date
2006-07-10
Thiol separation (Å)
2
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q91WY9
Residue number A
34
Residue number B
31
Peptide name
Bone morphogenetic protein type II receptor
Ligandability
Cysteine 34 of Bone morphogenetic protein type II receptor
Cysteine 31 of Bone morphogenetic protein type II receptor
Cysteine 34 in protein A could not be asigned to a Uniprot residue.
2hlr A 94 A 117
A redox-regulated disulphide may form within Bone morphogenetic protein type II receptor between cysteines 59 and 82 (94 and 117 respectively in this structure).
Details
Redox score ?
81
PDB code
2hlr
Structure name
crystal structure of the extracellular domain of the type ii bmp receptor
Structure deposition date
2006-07-10
Thiol separation (Å)
2
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q91WY9
Residue number A
59
Residue number B
82
Peptide name
Bone morphogenetic protein type II receptor
Ligandability
Cysteine 59 of Bone morphogenetic protein type II receptor
Cysteine 82 of Bone morphogenetic protein type II receptor
2hlr A 34 A 60
A redox-regulated disulphide may form within Bone morphogenetic protein type II receptor between cysteines 34 and 25 (34 and 60 respectively in this structure).
Details
Redox score ?
80
PDB code
2hlr
Structure name
crystal structure of the extracellular domain of the type ii bmp receptor
Structure deposition date
2006-07-10
Thiol separation (Å)
3
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q91WY9
Residue number A
34
Residue number B
25
Peptide name
Bone morphogenetic protein type II receptor
Ligandability
Cysteine 34 of Bone morphogenetic protein type II receptor
Cysteine 25 of Bone morphogenetic protein type II receptor
Cysteine 34 in protein A could not be asigned to a Uniprot residue.
2hlr A 118 A 123
A redox-regulated disulphide may form within Bone morphogenetic protein type II receptor between cysteines 83 and 88 (118 and 123 respectively in this structure).
Details
Redox score ?
78
PDB code
2hlr
Structure name
crystal structure of the extracellular domain of the type ii bmp receptor
Structure deposition date
2006-07-10
Thiol separation (Å)
2
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q91WY9
Residue number A
83
Residue number B
88
Peptide name
Bone morphogenetic protein type II receptor
Ligandability
Cysteine 83 of Bone morphogenetic protein type II receptor
Cysteine 88 of Bone morphogenetic protein type II receptor
2hlr A 99 A 118
A redox-regulated disulphide may form within Bone morphogenetic protein type II receptor between cysteines 64 and 83 (99 and 118 respectively in this structure).
Details
Redox score ?
72
PDB code
2hlr
Structure name
crystal structure of the extracellular domain of the type ii bmp receptor
Structure deposition date
2006-07-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q91WY9
Residue number A
64
Residue number B
83
Peptide name
Bone morphogenetic protein type II receptor
Ligandability
Cysteine 64 of Bone morphogenetic protein type II receptor
Cysteine 83 of Bone morphogenetic protein type II receptor
2hlr A 66 A 123
A redox-regulated disulphide may form within Bone morphogenetic protein type II receptor between cysteines 31 and 88 (66 and 123 respectively in this structure).
Details
Redox score ?
68
PDB code
2hlr
Structure name
crystal structure of the extracellular domain of the type ii bmp receptor
Structure deposition date
2006-07-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q91WY9
Residue number A
31
Residue number B
88
Peptide name
Bone morphogenetic protein type II receptor
Ligandability
Cysteine 31 of Bone morphogenetic protein type II receptor
Cysteine 88 of Bone morphogenetic protein type II receptor
2hlr A 60 A 66
A redox-regulated disulphide may form within Bone morphogenetic protein type II receptor between cysteines 25 and 31 (60 and 66 respectively in this structure).
Details
Redox score ?
66
PDB code
2hlr
Structure name
crystal structure of the extracellular domain of the type ii bmp receptor
Structure deposition date
2006-07-10
Thiol separation (Å)
5
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q91WY9
Residue number A
25
Residue number B
31
Peptide name
Bone morphogenetic protein type II receptor
Ligandability
Cysteine 25 of Bone morphogenetic protein type II receptor
Cysteine 31 of Bone morphogenetic protein type II receptor
2hlr A 34 A 84
A redox-regulated disulphide may form within Bone morphogenetic protein type II receptor between cysteines 34 and 49 (34 and 84 respectively in this structure).
Details
Redox score ?
65
PDB code
2hlr
Structure name
crystal structure of the extracellular domain of the type ii bmp receptor
Structure deposition date
2006-07-10
Thiol separation (Å)
5
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q91WY9
Residue number A
34
Residue number B
49
Peptide name
Bone morphogenetic protein type II receptor
Ligandability
Cysteine 34 of Bone morphogenetic protein type II receptor
Cysteine 49 of Bone morphogenetic protein type II receptor
Cysteine 34 in protein A could not be asigned to a Uniprot residue.
2hlr A 99 A 123
A redox-regulated disulphide may form within Bone morphogenetic protein type II receptor between cysteines 64 and 88 (99 and 123 respectively in this structure).
Details
Redox score ?
62
PDB code
2hlr
Structure name
crystal structure of the extracellular domain of the type ii bmp receptor
Structure deposition date
2006-07-10
Thiol separation (Å)
6
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q91WY9
Residue number A
64
Residue number B
88
Peptide name
Bone morphogenetic protein type II receptor
Ligandability
Cysteine 64 of Bone morphogenetic protein type II receptor
Cysteine 88 of Bone morphogenetic protein type II receptor
2hlr A 66 A 118
A redox-regulated disulphide may form within Bone morphogenetic protein type II receptor between cysteines 31 and 83 (66 and 118 respectively in this structure).
Details
Redox score ?
60
PDB code
2hlr
Structure name
crystal structure of the extracellular domain of the type ii bmp receptor
Structure deposition date
2006-07-10
Thiol separation (Å)
5
Half-sphere exposure sum ?
87
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q91WY9
Residue number A
31
Residue number B
83
Peptide name
Bone morphogenetic protein type II receptor
Ligandability
Cysteine 31 of Bone morphogenetic protein type II receptor
Cysteine 83 of Bone morphogenetic protein type II receptor
2hlr A 34 A 123
A redox-regulated disulphide may form within Bone morphogenetic protein type II receptor between cysteines 34 and 88 (34 and 123 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
59
PDB code
2hlr
Structure name
crystal structure of the extracellular domain of the type ii bmp receptor
Structure deposition date
2006-07-10
Thiol separation (Å)
6
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q91WY9
Residue number A
34
Residue number B
88
Peptide name
Bone morphogenetic protein type II receptor
Ligandability
Cysteine 34 of Bone morphogenetic protein type II receptor
Cysteine 88 of Bone morphogenetic protein type II receptor
Cysteine 34 in protein A could not be asigned to a Uniprot residue.
2hlr A 116 A 118
A redox-regulated disulphide may form within Bone morphogenetic protein type II receptor between cysteines 81 and 83 (116 and 118 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
2hlr
Structure name
crystal structure of the extracellular domain of the type ii bmp receptor
Structure deposition date
2006-07-10
Thiol separation (Å)
6
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q91WY9
Residue number A
81
Residue number B
83
Peptide name
Bone morphogenetic protein type II receptor
Ligandability
Cysteine 81 of Bone morphogenetic protein type II receptor
Cysteine 83 of Bone morphogenetic protein type II receptor
2hlr A 34 A 118
A redox-regulated disulphide may form within Bone morphogenetic protein type II receptor between cysteines 34 and 83 (34 and 118 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
2hlr
Structure name
crystal structure of the extracellular domain of the type ii bmp receptor
Structure deposition date
2006-07-10
Thiol separation (Å)
7
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q91WY9
Residue number A
34
Residue number B
83
Peptide name
Bone morphogenetic protein type II receptor
Ligandability
Cysteine 34 of Bone morphogenetic protein type II receptor
Cysteine 83 of Bone morphogenetic protein type II receptor
Cysteine 34 in protein A could not be asigned to a Uniprot residue.
2hlr A 99 A 117
A redox-regulated disulphide may form within Bone morphogenetic protein type II receptor between cysteines 64 and 82 (99 and 117 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
2hlr
Structure name
crystal structure of the extracellular domain of the type ii bmp receptor
Structure deposition date
2006-07-10
Thiol separation (Å)
7
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q91WY9
Residue number A
64
Residue number B
82
Peptide name
Bone morphogenetic protein type II receptor
Ligandability
Cysteine 64 of Bone morphogenetic protein type II receptor
Cysteine 82 of Bone morphogenetic protein type II receptor
2hlr A 94 A 99
A redox-regulated disulphide may form within Bone morphogenetic protein type II receptor between cysteines 59 and 64 (94 and 99 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
2hlr
Structure name
crystal structure of the extracellular domain of the type ii bmp receptor
Structure deposition date
2006-07-10
Thiol separation (Å)
8
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q91WY9
Residue number A
59
Residue number B
64
Peptide name
Bone morphogenetic protein type II receptor
Ligandability
Cysteine 59 of Bone morphogenetic protein type II receptor
Cysteine 64 of Bone morphogenetic protein type II receptor
2hlr A 94 A 118
A redox-regulated disulphide may form within Bone morphogenetic protein type II receptor between cysteines 59 and 83 (94 and 118 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
2hlr
Structure name
crystal structure of the extracellular domain of the type ii bmp receptor
Structure deposition date
2006-07-10
Thiol separation (Å)
7
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q91WY9
Residue number A
59
Residue number B
83
Peptide name
Bone morphogenetic protein type II receptor
Ligandability
Cysteine 59 of Bone morphogenetic protein type II receptor
Cysteine 83 of Bone morphogenetic protein type II receptor
2hlr A 66 A 84
A redox-regulated disulphide may form within Bone morphogenetic protein type II receptor between cysteines 31 and 49 (66 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 ?
50
PDB code
2hlr
Structure name
crystal structure of the extracellular domain of the type ii bmp receptor
Structure deposition date
2006-07-10
Thiol separation (Å)
7
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q91WY9
Residue number A
31
Residue number B
49
Peptide name
Bone morphogenetic protein type II receptor
Ligandability
Cysteine 31 of Bone morphogenetic protein type II receptor
Cysteine 49 of Bone morphogenetic protein type II receptor
2hlr A 66 A 99
A redox-regulated disulphide may form within Bone morphogenetic protein type II receptor between cysteines 31 and 64 (66 and 99 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
2hlr
Structure name
crystal structure of the extracellular domain of the type ii bmp receptor
Structure deposition date
2006-07-10
Thiol separation (Å)
8
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q91WY9
Residue number A
31
Residue number B
64
Peptide name
Bone morphogenetic protein type II receptor
Ligandability
Cysteine 31 of Bone morphogenetic protein type II receptor
Cysteine 64 of Bone morphogenetic protein type II receptor
2hlr A 116 A 123
A redox-regulated disulphide may form within Bone morphogenetic protein type II receptor between cysteines 81 and 88 (116 and 123 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
2hlr
Structure name
crystal structure of the extracellular domain of the type ii bmp receptor
Structure deposition date
2006-07-10
Thiol separation (Å)
8
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q91WY9
Residue number A
81
Residue number B
88
Peptide name
Bone morphogenetic protein type II receptor
Ligandability
Cysteine 81 of Bone morphogenetic protein type II receptor
Cysteine 88 of Bone morphogenetic protein type II receptor
2hlr A 116 A 117
A redox-regulated disulphide may form within Bone morphogenetic protein type II receptor between cysteines 81 and 82 (116 and 117 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
2hlr
Structure name
crystal structure of the extracellular domain of the type ii bmp receptor
Structure deposition date
2006-07-10
Thiol separation (Å)
7
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q91WY9
Residue number A
81
Residue number B
82
Peptide name
Bone morphogenetic protein type II receptor
Ligandability
Cysteine 81 of Bone morphogenetic protein type II receptor
Cysteine 82 of Bone morphogenetic protein type II receptor
2hlr A 117 A 118
A redox-regulated disulphide may form within Bone morphogenetic protein type II receptor between cysteines 82 and 83 (117 and 118 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
2hlr
Structure name
crystal structure of the extracellular domain of the type ii bmp receptor
Structure deposition date
2006-07-10
Thiol separation (Å)
7
Half-sphere exposure sum ?
85
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q91WY9
Residue number A
82
Residue number B
83
Peptide name
Bone morphogenetic protein type II receptor
Ligandability
Cysteine 82 of Bone morphogenetic protein type II receptor
Cysteine 83 of Bone morphogenetic protein type II receptor
2hlr A 94 A 123
A redox-regulated disulphide may form within Bone morphogenetic protein type II receptor between cysteines 59 and 88 (94 and 123 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
2hlr
Structure name
crystal structure of the extracellular domain of the type ii bmp receptor
Structure deposition date
2006-07-10
Thiol separation (Å)
8
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q91WY9
Residue number A
59
Residue number B
88
Peptide name
Bone morphogenetic protein type II receptor
Ligandability
Cysteine 59 of Bone morphogenetic protein type II receptor
Cysteine 88 of Bone morphogenetic protein type II receptor
2hlr A 94 A 116
A redox-regulated disulphide may form within Bone morphogenetic protein type II receptor between cysteines 59 and 81 (94 and 116 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
2hlr
Structure name
crystal structure of the extracellular domain of the type ii bmp receptor
Structure deposition date
2006-07-10
Thiol separation (Å)
9
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q91WY9
Residue number A
59
Residue number B
81
Peptide name
Bone morphogenetic protein type II receptor
Ligandability
Cysteine 59 of Bone morphogenetic protein type II receptor
Cysteine 81 of Bone morphogenetic protein type II receptor
2hlr A 34 A 99
A redox-regulated disulphide may form within Bone morphogenetic protein type II receptor between cysteines 34 and 64 (34 and 99 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
2hlr
Structure name
crystal structure of the extracellular domain of the type ii bmp receptor
Structure deposition date
2006-07-10
Thiol separation (Å)
10
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q91WY9
Residue number A
34
Residue number B
64
Peptide name
Bone morphogenetic protein type II receptor
Ligandability
Cysteine 34 of Bone morphogenetic protein type II receptor
Cysteine 64 of Bone morphogenetic protein type II receptor
Cysteine 34 in protein A could not be asigned to a Uniprot residue.
2hlr A 60 A 123
A redox-regulated disulphide may form within Bone morphogenetic protein type II receptor between cysteines 25 and 88 (60 and 123 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
2hlr
Structure name
crystal structure of the extracellular domain of the type ii bmp receptor
Structure deposition date
2006-07-10
Thiol separation (Å)
9
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q91WY9
Residue number A
25
Residue number B
88
Peptide name
Bone morphogenetic protein type II receptor
Ligandability
Cysteine 25 of Bone morphogenetic protein type II receptor
Cysteine 88 of Bone morphogenetic protein type II receptor
2hlr A 66 A 94
A redox-regulated disulphide may form within Bone morphogenetic protein type II receptor between cysteines 31 and 59 (66 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 ?
42
PDB code
2hlr
Structure name
crystal structure of the extracellular domain of the type ii bmp receptor
Structure deposition date
2006-07-10
Thiol separation (Å)
9
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q91WY9
Residue number A
31
Residue number B
59
Peptide name
Bone morphogenetic protein type II receptor
Ligandability
Cysteine 31 of Bone morphogenetic protein type II receptor
Cysteine 59 of Bone morphogenetic protein type II receptor
2hlr A 34 A 94
A redox-regulated disulphide may form within Bone morphogenetic protein type II receptor between cysteines 34 and 59 (34 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 ?
40
PDB code
2hlr
Structure name
crystal structure of the extracellular domain of the type ii bmp receptor
Structure deposition date
2006-07-10
Thiol separation (Å)
10
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q91WY9
Residue number A
34
Residue number B
59
Peptide name
Bone morphogenetic protein type II receptor
Ligandability
Cysteine 34 of Bone morphogenetic protein type II receptor
Cysteine 59 of Bone morphogenetic protein type II receptor
Cysteine 34 in protein A could not be asigned to a Uniprot residue.
2hlr A 117 A 123
A redox-regulated disulphide may form within Bone morphogenetic protein type II receptor between cysteines 82 and 88 (117 and 123 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
2hlr
Structure name
crystal structure of the extracellular domain of the type ii bmp receptor
Structure deposition date
2006-07-10
Thiol separation (Å)
8
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q91WY9
Residue number A
82
Residue number B
88
Peptide name
Bone morphogenetic protein type II receptor
Ligandability
Cysteine 82 of Bone morphogenetic protein type II receptor
Cysteine 88 of Bone morphogenetic protein type II receptor
2hlr A 66 A 116
A redox-regulated disulphide may form within Bone morphogenetic protein type II receptor between cysteines 31 and 81 (66 and 116 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
35
PDB code
2hlr
Structure name
crystal structure of the extracellular domain of the type ii bmp receptor
Structure deposition date
2006-07-10
Thiol separation (Å)
10
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q91WY9
Residue number A
31
Residue number B
81
Peptide name
Bone morphogenetic protein type II receptor
Ligandability
Cysteine 31 of Bone morphogenetic protein type II receptor
Cysteine 81 of Bone morphogenetic protein type II receptor
2hlr A 66 A 117
A redox-regulated disulphide may form within Bone morphogenetic protein type II receptor between cysteines 31 and 82 (66 and 117 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
35
PDB code
2hlr
Structure name
crystal structure of the extracellular domain of the type ii bmp receptor
Structure deposition date
2006-07-10
Thiol separation (Å)
9
Half-sphere exposure sum ?
90
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q91WY9
Residue number A
31
Residue number B
82
Peptide name
Bone morphogenetic protein type II receptor
Ligandability
Cysteine 31 of Bone morphogenetic protein type II receptor
Cysteine 82 of Bone morphogenetic protein type II receptor
If this tool was useful for finding a disulphide, please cite: