Gremlin-1
Intermolecular
Cysteine 141 and cysteine 141
Cysteine 178 and cysteine 141
Cysteine 141 and cysteine 122
Cysteine 122 and cysteine 122
Cysteine 141 and cysteine 144
Intramolecular
Cysteine 108 and cysteine 158
Cysteine 94 and cysteine 144
Cysteine 122 and cysteine 178
Cysteine 118 and cysteine 176
Cysteine 94 and cysteine 178
More...Cysteine 94 and cysteine 176
Cysteine 94 and cysteine 122
Cysteine 144 and cysteine 176
Cysteine 144 and cysteine 178
Cysteine 122 and cysteine 144
Cysteine 94 and cysteine 118
Cysteine 118 and cysteine 144
Cysteine 176 and cysteine 178
Cysteine 122 and cysteine 176
Cysteine 118 and cysteine 178
Cysteine 118 and cysteine 122
5aej C 141 D 141
A redox-regulated disulphide may form between two units of Gremlin-1 at cysteines 141 and 141.
Details
Redox score ?
69
PDB code
5aej
Structure name
crystal structure of human gremlin-1
Structure deposition date
2015-08-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
77
Minimum pKa ?
9
% buried
98
Peptide A name
Gremlin-1
Peptide B name
Gremlin-1
Peptide A accession
O60565
Peptide B accession
O60565
Peptide A residue number
141
Peptide B residue number
141
Ligandability
5aej A 178 B 141
A redox-regulated disulphide may form between two units of Gremlin-1 at cysteines 178 and 141. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
5aej
Structure name
crystal structure of human gremlin-1
Structure deposition date
2015-08-31
Thiol separation (Å)
9
Half-sphere exposure sum ?
74
Minimum pKa ?
9
% buried
nan
Peptide A name
Gremlin-1
Peptide B name
Gremlin-1
Peptide A accession
O60565
Peptide B accession
O60565
Peptide A residue number
178
Peptide B residue number
141
Ligandability
Cysteine 178 of Gremlin-1
Cysteine 141 of Gremlin-1
5aej C 141 D 122
A redox-regulated disulphide may form between two units of Gremlin-1 at cysteines 141 and 122. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
36
PDB code
5aej
Structure name
crystal structure of human gremlin-1
Structure deposition date
2015-08-31
Thiol separation (Å)
7
Half-sphere exposure sum ?
79
Minimum pKa ?
18
% buried
nan
Peptide A name
Gremlin-1
Peptide B name
Gremlin-1
Peptide A accession
O60565
Peptide B accession
O60565
Peptide A residue number
141
Peptide B residue number
122
Ligandability
Cysteine 141 of Gremlin-1
Cysteine 122 of Gremlin-1
5aej A 122 B 122
A redox-regulated disulphide may form between two units of Gremlin-1 at cysteines 122 and 122. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
5aej
Structure name
crystal structure of human gremlin-1
Structure deposition date
2015-08-31
Thiol separation (Å)
10
Half-sphere exposure sum ?
84
Minimum pKa ?
nan
% buried
nan
Peptide A name
Gremlin-1
Peptide B name
Gremlin-1
Peptide A accession
O60565
Peptide B accession
O60565
Peptide A residue number
122
Peptide B residue number
122
Ligandability
5aej A 141 B 144
A redox-regulated disulphide may form between two units of Gremlin-1 at cysteines 141 and 144. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
24
PDB code
5aej
Structure name
crystal structure of human gremlin-1
Structure deposition date
2015-08-31
Thiol separation (Å)
9
Half-sphere exposure sum ?
78
Minimum pKa ?
18
% buried
nan
Peptide A name
Gremlin-1
Peptide B name
Gremlin-1
Peptide A accession
O60565
Peptide B accession
O60565
Peptide A residue number
141
Peptide B residue number
144
Ligandability
Cysteine 141 of Gremlin-1
Cysteine 144 of Gremlin-1
5aej C 108 C 158
A redox-regulated disulphide may form within Gremlin-1 between cysteines 108 and 158.
Details
Redox score ?
89
PDB code
5aej
Structure name
crystal structure of human gremlin-1
Structure deposition date
2015-08-31
Thiol separation (Å)
2
Half-sphere exposure sum ?
43
Minimum pKa ?
nan
% buried
nan
Peptide accession
O60565
Residue number A
108
Residue number B
158
Peptide name
Gremlin-1
Ligandability
Cysteine 108 of Gremlin-1
Cysteine 158 of Gremlin-1
5aej D 94 D 144
A redox-regulated disulphide may form within Gremlin-1 between cysteines 94 and 144.
Details
Redox score ?
85
PDB code
5aej
Structure name
crystal structure of human gremlin-1
Structure deposition date
2015-08-31
Thiol separation (Å)
2
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
O60565
Residue number A
94
Residue number B
144
Peptide name
Gremlin-1
Ligandability
Cysteine 94 of Gremlin-1
Cysteine 144 of Gremlin-1
5aej D 122 D 178
A redox-regulated disulphide may form within Gremlin-1 between cysteines 122 and 178.
Details
Redox score ?
82
PDB code
5aej
Structure name
crystal structure of human gremlin-1
Structure deposition date
2015-08-31
Thiol separation (Å)
2
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
O60565
Residue number A
122
Residue number B
178
Peptide name
Gremlin-1
Ligandability
Cysteine 122 of Gremlin-1
Cysteine 178 of Gremlin-1
5aej B 118 B 176
A redox-regulated disulphide may form within Gremlin-1 between cysteines 118 and 176.
Details
Redox score ?
82
PDB code
5aej
Structure name
crystal structure of human gremlin-1
Structure deposition date
2015-08-31
Thiol separation (Å)
2
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
O60565
Residue number A
118
Residue number B
176
Peptide name
Gremlin-1
Ligandability
Cysteine 118 of Gremlin-1
Cysteine 176 of Gremlin-1
5aej C 94 C 178
A redox-regulated disulphide may form within Gremlin-1 between cysteines 94 and 178.
Details
Redox score ?
71
PDB code
5aej
Structure name
crystal structure of human gremlin-1
Structure deposition date
2015-08-31
Thiol separation (Å)
5
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
O60565
Residue number A
94
Residue number B
178
Peptide name
Gremlin-1
Ligandability
Cysteine 94 of Gremlin-1
Cysteine 178 of Gremlin-1
5aej C 94 C 176
A redox-regulated disulphide may form within Gremlin-1 between cysteines 94 and 176.
Details
Redox score ?
70
PDB code
5aej
Structure name
crystal structure of human gremlin-1
Structure deposition date
2015-08-31
Thiol separation (Å)
5
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
O60565
Residue number A
94
Residue number B
176
Peptide name
Gremlin-1
Ligandability
Cysteine 94 of Gremlin-1
Cysteine 176 of Gremlin-1
5aej A 94 A 122
A redox-regulated disulphide may form within Gremlin-1 between cysteines 94 and 122.
Details
Redox score ?
67
PDB code
5aej
Structure name
crystal structure of human gremlin-1
Structure deposition date
2015-08-31
Thiol separation (Å)
5
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
O60565
Residue number A
94
Residue number B
122
Peptide name
Gremlin-1
Ligandability
Cysteine 94 of Gremlin-1
Cysteine 122 of Gremlin-1
5aej A 144 A 176
A redox-regulated disulphide may form within Gremlin-1 between cysteines 144 and 176.
Details
Redox score ?
66
PDB code
5aej
Structure name
crystal structure of human gremlin-1
Structure deposition date
2015-08-31
Thiol separation (Å)
5
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
O60565
Residue number A
144
Residue number B
176
Peptide name
Gremlin-1
Ligandability
Cysteine 144 of Gremlin-1
Cysteine 176 of Gremlin-1
5aej B 144 B 178
A redox-regulated disulphide may form within Gremlin-1 between cysteines 144 and 178.
Details
Redox score ?
65
PDB code
5aej
Structure name
crystal structure of human gremlin-1
Structure deposition date
2015-08-31
Thiol separation (Å)
5
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
O60565
Residue number A
144
Residue number B
178
Peptide name
Gremlin-1
Ligandability
Cysteine 144 of Gremlin-1
Cysteine 178 of Gremlin-1
5aej D 122 D 144
A redox-regulated disulphide may form within Gremlin-1 between cysteines 122 and 144.
Details
Redox score ?
63
PDB code
5aej
Structure name
crystal structure of human gremlin-1
Structure deposition date
2015-08-31
Thiol separation (Å)
5
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
O60565
Residue number A
122
Residue number B
144
Peptide name
Gremlin-1
Ligandability
Cysteine 122 of Gremlin-1
Cysteine 144 of Gremlin-1
5aej A 94 A 118
A redox-regulated disulphide may form within Gremlin-1 between cysteines 94 and 118.
Details
Redox score ?
61
PDB code
5aej
Structure name
crystal structure of human gremlin-1
Structure deposition date
2015-08-31
Thiol separation (Å)
6
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
O60565
Residue number A
94
Residue number B
118
Peptide name
Gremlin-1
Ligandability
Cysteine 94 of Gremlin-1
Cysteine 118 of Gremlin-1
5aej A 118 A 144
A redox-regulated disulphide may form within Gremlin-1 between cysteines 118 and 144.
Details
Redox score ?
61
PDB code
5aej
Structure name
crystal structure of human gremlin-1
Structure deposition date
2015-08-31
Thiol separation (Å)
5
Half-sphere exposure sum ?
85
Minimum pKa ?
nan
% buried
nan
Peptide accession
O60565
Residue number A
118
Residue number B
144
Peptide name
Gremlin-1
Ligandability
Cysteine 118 of Gremlin-1
Cysteine 144 of Gremlin-1
5aej A 176 A 178
A redox-regulated disulphide may form within Gremlin-1 between cysteines 176 and 178. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
5aej
Structure name
crystal structure of human gremlin-1
Structure deposition date
2015-08-31
Thiol separation (Å)
10
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
O60565
Residue number A
176
Residue number B
178
Peptide name
Gremlin-1
Ligandability
Cysteine 176 of Gremlin-1
Cysteine 178 of Gremlin-1
5aej A 122 A 176
A redox-regulated disulphide may form within Gremlin-1 between cysteines 122 and 176. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
5aej
Structure name
crystal structure of human gremlin-1
Structure deposition date
2015-08-31
Thiol separation (Å)
10
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
O60565
Residue number A
122
Residue number B
176
Peptide name
Gremlin-1
Ligandability
Cysteine 122 of Gremlin-1
Cysteine 176 of Gremlin-1
5aej C 118 C 178
A redox-regulated disulphide may form within Gremlin-1 between cysteines 118 and 178. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
35
PDB code
5aej
Structure name
crystal structure of human gremlin-1
Structure deposition date
2015-08-31
Thiol separation (Å)
10
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
O60565
Residue number A
118
Residue number B
178
Peptide name
Gremlin-1
Ligandability
Cysteine 118 of Gremlin-1
Cysteine 178 of Gremlin-1
5aej C 118 C 122
A redox-regulated disulphide may form within Gremlin-1 between cysteines 118 and 122. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
5aej
Structure name
crystal structure of human gremlin-1
Structure deposition date
2015-08-31
Thiol separation (Å)
10
Half-sphere exposure sum ?
87
Minimum pKa ?
nan
% buried
nan
Peptide accession
O60565
Residue number A
118
Residue number B
122
Peptide name
Gremlin-1
Ligandability
Cysteine 118 of Gremlin-1
Cysteine 122 of Gremlin-1
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