Follistatin
Intramolecular
Cysteine 95 and cysteine 106
Cysteine 100 and cysteine 116
Cysteine 196 and cysteine 218
Cysteine 122 and cysteine 143
Cysteine 245 and cysteine 256
Cysteine 168 and cysteine 179
Cysteine 173 and cysteine 189
Cysteine 118 and cysteine 150
Cysteine 192 and cysteine 225
Cysteine 284 and cysteine 316
More...Cysteine 207 and cysteine 239
Cysteine 56 and cysteine 91
Cysteine 132 and cysteine 164
Cysteine 42 and cysteine 88
Cysteine 32 and cysteine 55
Cysteine 250 and cysteine 267
Cysteine 270 and cysteine 302
Cysteine 55 and cysteine 91
Cysteine 100 and cysteine 106
Cysteine 274 and cysteine 295
Cysteine 55 and cysteine 56
Cysteine 173 and cysteine 179
Cysteine 250 and cysteine 256
Cysteine 106 and cysteine 116
Cysteine 179 and cysteine 189
Cysteine 245 and cysteine 250
Cysteine 256 and cysteine 267
Cysteine 168 and cysteine 173
Cysteine 95 and cysteine 100
Cysteine 95 and cysteine 116
Cysteine 168 and cysteine 189
Cysteine 245 and cysteine 267
Cysteine 32 and cysteine 91
Cysteine 270 and cysteine 295
Cysteine 250 and cysteine 270
Cysteine 132 and cysteine 189
Cysteine 173 and cysteine 192
Cysteine 274 and cysteine 302
Cysteine 55 and cysteine 88
Cysteine 32 and cysteine 56
5jhw C 66 C 77
A redox-regulated disulphide may form within Follistatin between cysteines 95 and 106 (66 and 77 respectively in this structure).
Details
Redox score ?
88
PDB code
5jhw
Structure name
crystal structure of the gdf11:follistatin 288 complex
Structure deposition date
2016-04-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19883
Residue number A
95
Residue number B
106
Peptide name
Follistatin
Ligandability
Cysteine 95 of Follistatin
Cysteine 106 of Follistatin
5jhw C 71 C 87
A redox-regulated disulphide may form within Follistatin between cysteines 100 and 116 (71 and 87 respectively in this structure).
Details
Redox score ?
87
PDB code
5jhw
Structure name
crystal structure of the gdf11:follistatin 288 complex
Structure deposition date
2016-04-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19883
Residue number A
100
Residue number B
116
Peptide name
Follistatin
Ligandability
Cysteine 100 of Follistatin
Cysteine 116 of Follistatin
5jhw C 167 C 189
A redox-regulated disulphide may form within Follistatin between cysteines 196 and 218 (167 and 189 respectively in this structure).
Details
Redox score ?
87
PDB code
5jhw
Structure name
crystal structure of the gdf11:follistatin 288 complex
Structure deposition date
2016-04-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19883
Residue number A
196
Residue number B
218
Peptide name
Follistatin
Ligandability
Cysteine 196 of Follistatin
Cysteine 218 of Follistatin
1lr8 A 93 A 114
A redox-regulated disulphide may form within Follistatin between cysteines 122 and 143 (93 and 114 respectively in this structure).
Details
Redox score ?
86
PDB code
1lr8
Structure name
crystal structure of fs1, the heparin-binding domain of follistatin, complexed with the heparin analogue d-myo-inositol hexasulphate (ins6s)
Structure deposition date
2002-05-15
Thiol separation (Å)
2
Half-sphere exposure sum ?
47
Minimum pKa ?
nan
% buried
nan
Peptide accession
P21674
Residue number A
122
Residue number B
143
Peptide name
Follistatin
Ligandability
Cysteine 122 of Follistatin
Cysteine 143 of Follistatin
2p6a C 216 C 227
A redox-regulated disulphide may form within Follistatin between cysteines 245 and 256 (216 and 227 respectively in this structure).
Details
Redox score ?
86
PDB code
2p6a
Structure name
the structure of the activin:follistatin 315 complex
Structure deposition date
2007-03-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19883
Residue number A
245
Residue number B
256
Peptide name
Follistatin
Ligandability
Cysteine 245 of Follistatin
Cysteine 256 of Follistatin
5jhw C 139 C 150
A redox-regulated disulphide may form within Follistatin between cysteines 168 and 179 (139 and 150 respectively in this structure).
Details
Redox score ?
85
PDB code
5jhw
Structure name
crystal structure of the gdf11:follistatin 288 complex
Structure deposition date
2016-04-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19883
Residue number A
168
Residue number B
179
Peptide name
Follistatin
Ligandability
Cysteine 168 of Follistatin
Cysteine 179 of Follistatin
5jhw C 144 C 160
A redox-regulated disulphide may form within Follistatin between cysteines 173 and 189 (144 and 160 respectively in this structure).
Details
Redox score ?
84
PDB code
5jhw
Structure name
crystal structure of the gdf11:follistatin 288 complex
Structure deposition date
2016-04-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19883
Residue number A
173
Residue number B
189
Peptide name
Follistatin
Ligandability
Cysteine 173 of Follistatin
Cysteine 189 of Follistatin
1lr9 A 89 A 121
A redox-regulated disulphide may form within Follistatin between cysteines 118 and 150 (89 and 121 respectively in this structure).
Details
Redox score ?
84
PDB code
1lr9
Structure name
structure of fs1, the heparin-binding domain of follistatin
Structure deposition date
2002-05-15
Thiol separation (Å)
2
Half-sphere exposure sum ?
47
Minimum pKa ?
nan
% buried
nan
Peptide accession
P21674
Residue number A
118
Residue number B
150
Peptide name
Follistatin
Ligandability
Cysteine 118 of Follistatin
Cysteine 150 of Follistatin
5jhw D 163 D 196
A redox-regulated disulphide may form within Follistatin between cysteines 192 and 225 (163 and 196 respectively in this structure).
Details
Redox score ?
84
PDB code
5jhw
Structure name
crystal structure of the gdf11:follistatin 288 complex
Structure deposition date
2016-04-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19883
Residue number A
192
Residue number B
225
Peptide name
Follistatin
Ligandability
Cysteine 192 of Follistatin
Cysteine 225 of Follistatin
2p6a C 255 C 287
A redox-regulated disulphide may form within Follistatin between cysteines 284 and 316 (255 and 287 respectively in this structure).
Details
Redox score ?
83
PDB code
2p6a
Structure name
the structure of the activin:follistatin 315 complex
Structure deposition date
2007-03-16
Thiol separation (Å)
4
Half-sphere exposure sum ?
44
Minimum pKa ?
8
% buried
0
Peptide accession
P19883
Residue number A
284
Residue number B
316
Peptide name
Follistatin
Ligandability
Cysteine 284 of Follistatin
Cysteine 316 of Follistatin
5jhw D 178 D 210
A redox-regulated disulphide may form within Follistatin between cysteines 207 and 239 (178 and 210 respectively in this structure).
Details
Redox score ?
83
PDB code
5jhw
Structure name
crystal structure of the gdf11:follistatin 288 complex
Structure deposition date
2016-04-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19883
Residue number A
207
Residue number B
239
Peptide name
Follistatin
Ligandability
Cysteine 207 of Follistatin
Cysteine 239 of Follistatin
5jhw C 27 C 62
A redox-regulated disulphide may form within Follistatin between cysteines 56 and 91 (27 and 62 respectively in this structure).
Details
Redox score ?
83
PDB code
5jhw
Structure name
crystal structure of the gdf11:follistatin 288 complex
Structure deposition date
2016-04-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19883
Residue number A
56
Residue number B
91
Peptide name
Follistatin
Ligandability
Cysteine 56 of Follistatin
Cysteine 91 of Follistatin
5jhw C 103 C 135
A redox-regulated disulphide may form within Follistatin between cysteines 132 and 164 (103 and 135 respectively in this structure).
Details
Redox score ?
83
PDB code
5jhw
Structure name
crystal structure of the gdf11:follistatin 288 complex
Structure deposition date
2016-04-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19883
Residue number A
132
Residue number B
164
Peptide name
Follistatin
Ligandability
Cysteine 132 of Follistatin
Cysteine 164 of Follistatin
5jhw C 13 C 59
A redox-regulated disulphide may form within Follistatin between cysteines 42 and 88 (13 and 59 respectively in this structure).
Details
Redox score ?
82
PDB code
5jhw
Structure name
crystal structure of the gdf11:follistatin 288 complex
Structure deposition date
2016-04-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19883
Residue number A
42
Residue number B
88
Peptide name
Follistatin
Ligandability
Cysteine 42 of Follistatin
Cysteine 88 of Follistatin
5jhw C 3 C 26
A redox-regulated disulphide may form within Follistatin between cysteines 32 and 55 (3 and 26 respectively in this structure).
Details
Redox score ?
81
PDB code
5jhw
Structure name
crystal structure of the gdf11:follistatin 288 complex
Structure deposition date
2016-04-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19883
Residue number A
32
Residue number B
55
Peptide name
Follistatin
Ligandability
Cysteine 32 of Follistatin
Cysteine 55 of Follistatin
2p6a C 221 C 238
A redox-regulated disulphide may form within Follistatin between cysteines 250 and 267 (221 and 238 respectively in this structure).
Details
Redox score ?
79
PDB code
2p6a
Structure name
the structure of the activin:follistatin 315 complex
Structure deposition date
2007-03-16
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
8
% buried
32
Peptide accession
P19883
Residue number A
250
Residue number B
267
Peptide name
Follistatin
Ligandability
Cysteine 250 of Follistatin
Cysteine 267 of Follistatin
2p6a D 241 D 273
A redox-regulated disulphide may form within Follistatin between cysteines 270 and 302 (241 and 273 respectively in this structure).
Details
Redox score ?
74
PDB code
2p6a
Structure name
the structure of the activin:follistatin 315 complex
Structure deposition date
2007-03-16
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
9
% buried
32
Peptide accession
P19883
Residue number A
270
Residue number B
302
Peptide name
Follistatin
Ligandability
Cysteine 270 of Follistatin
Cysteine 302 of Follistatin
2b0u C 26 C 62
A redox-regulated disulphide may form within Follistatin between cysteines 55 and 91 (26 and 62 respectively in this structure).
Details
Redox score ?
73
PDB code
2b0u
Structure name
the structure of the follistatin:activin complex
Structure deposition date
2005-09-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19883
Residue number A
55
Residue number B
91
Peptide name
Follistatin
Ligandability
Cysteine 55 of Follistatin
Cysteine 91 of Follistatin
1lr7 A 71 A 77
A redox-regulated disulphide may form within Follistatin between cysteines 100 and 106 (71 and 77 respectively in this structure).
Details
Redox score ?
73
PDB code
1lr7
Structure name
crystal structure of fs1, the heparin-binding domain of follistatin, complexed with the heparin analogue sucrose octasulphate (sos)
Structure deposition date
2002-05-15
Thiol separation (Å)
5
Half-sphere exposure sum ?
42
Minimum pKa ?
nan
% buried
nan
Peptide accession
P21674
Residue number A
100
Residue number B
106
Peptide name
Follistatin
Ligandability
Cysteine 100 of Follistatin
Cysteine 106 of Follistatin
2p6a D 245 D 266
A redox-regulated disulphide may form within Follistatin between cysteines 274 and 295 (245 and 266 respectively in this structure).
Details
Redox score ?
72
PDB code
2p6a
Structure name
the structure of the activin:follistatin 315 complex
Structure deposition date
2007-03-16
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
10
% buried
8
Peptide accession
P19883
Residue number A
274
Residue number B
295
Peptide name
Follistatin
Ligandability
Cysteine 274 of Follistatin
Cysteine 295 of Follistatin
3hh2 C 26 C 27
A redox-regulated disulphide may form within Follistatin between cysteines 55 and 56 (26 and 27 respectively in this structure).
Details
Redox score ?
72
PDB code
3hh2
Structure name
crystal structure of the myostatin:follistatin 288 complex
Structure deposition date
2009-05-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19883
Residue number A
55
Residue number B
56
Peptide name
Follistatin
Ligandability
Cysteine 55 of Follistatin
Cysteine 56 of Follistatin
2p6a D 144 D 150
A redox-regulated disulphide may form within Follistatin between cysteines 173 and 179 (144 and 150 respectively in this structure).
Details
Redox score ?
70
PDB code
2p6a
Structure name
the structure of the activin:follistatin 315 complex
Structure deposition date
2007-03-16
Thiol separation (Å)
5
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19883
Residue number A
173
Residue number B
179
Peptide name
Follistatin
Ligandability
Cysteine 173 of Follistatin
Cysteine 179 of Follistatin
3hh2 C 221 C 227
A redox-regulated disulphide may form within Follistatin between cysteines 250 and 256 (221 and 227 respectively in this structure).
Details
Redox score ?
69
PDB code
3hh2
Structure name
crystal structure of the myostatin:follistatin 288 complex
Structure deposition date
2009-05-14
Thiol separation (Å)
5
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19883
Residue number A
250
Residue number B
256
Peptide name
Follistatin
Ligandability
Cysteine 250 of Follistatin
Cysteine 256 of Follistatin
2arp F 77 F 87
A redox-regulated disulphide may form within Follistatin between cysteines 106 and 116 (77 and 87 respectively in this structure).
Details
Redox score ?
68
PDB code
2arp
Structure name
activin a in complex with fs12 fragment of follistatin
Structure deposition date
2005-08-21
Thiol separation (Å)
5
Half-sphere exposure sum ?
43
Minimum pKa ?
nan
% buried
nan
Peptide accession
P21674
Residue number A
106
Residue number B
116
Peptide name
Follistatin
Ligandability
Cysteine 106 of Follistatin
Cysteine 116 of Follistatin
2p6a D 150 D 160
A redox-regulated disulphide may form within Follistatin between cysteines 179 and 189 (150 and 160 respectively in this structure).
Details
Redox score ?
64
PDB code
2p6a
Structure name
the structure of the activin:follistatin 315 complex
Structure deposition date
2007-03-16
Thiol separation (Å)
5
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19883
Residue number A
179
Residue number B
189
Peptide name
Follistatin
Ligandability
Cysteine 179 of Follistatin
Cysteine 189 of Follistatin
2b0u C 216 C 221
A redox-regulated disulphide may form within Follistatin between cysteines 245 and 250 (216 and 221 respectively in this structure).
Details
Redox score ?
61
PDB code
2b0u
Structure name
the structure of the follistatin:activin complex
Structure deposition date
2005-09-14
Thiol separation (Å)
7
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19883
Residue number A
245
Residue number B
250
Peptide name
Follistatin
Ligandability
Cysteine 245 of Follistatin
Cysteine 250 of Follistatin
2p6a C 227 C 238
A redox-regulated disulphide may form within Follistatin between cysteines 256 and 267 (227 and 238 respectively in this structure).
Details
Redox score ?
61
PDB code
2p6a
Structure name
the structure of the activin:follistatin 315 complex
Structure deposition date
2007-03-16
Thiol separation (Å)
4
Half-sphere exposure sum ?
73
Minimum pKa ?
12
% buried
nan
Peptide accession
P19883
Residue number A
256
Residue number B
267
Peptide name
Follistatin
Ligandability
Cysteine 256 of Follistatin
Cysteine 267 of Follistatin
2p6a C 139 C 144
A redox-regulated disulphide may form within Follistatin between cysteines 168 and 173 (139 and 144 respectively in this structure).
Details
Redox score ?
60
PDB code
2p6a
Structure name
the structure of the activin:follistatin 315 complex
Structure deposition date
2007-03-16
Thiol separation (Å)
7
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19883
Residue number A
168
Residue number B
173
Peptide name
Follistatin
Ligandability
Cysteine 168 of Follistatin
Cysteine 173 of Follistatin
2b0u D 66 D 71
A redox-regulated disulphide may form within Follistatin between cysteines 95 and 100 (66 and 71 respectively in this structure).
Details
Redox score ?
60
PDB code
2b0u
Structure name
the structure of the follistatin:activin complex
Structure deposition date
2005-09-14
Thiol separation (Å)
7
Half-sphere exposure sum ?
46
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19883
Residue number A
95
Residue number B
100
Peptide name
Follistatin
Ligandability
Cysteine 95 of Follistatin
Cysteine 100 of Follistatin
3hh2 D 66 D 87
A redox-regulated disulphide may form within Follistatin between cysteines 95 and 116 (66 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 ?
56
PDB code
3hh2
Structure name
crystal structure of the myostatin:follistatin 288 complex
Structure deposition date
2009-05-14
Thiol separation (Å)
7
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19883
Residue number A
95
Residue number B
116
Peptide name
Follistatin
Ligandability
Cysteine 95 of Follistatin
Cysteine 116 of Follistatin
2p6a D 139 D 160
A redox-regulated disulphide may form within Follistatin between cysteines 168 and 189 (139 and 160 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
56
PDB code
2p6a
Structure name
the structure of the activin:follistatin 315 complex
Structure deposition date
2007-03-16
Thiol separation (Å)
7
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19883
Residue number A
168
Residue number B
189
Peptide name
Follistatin
Ligandability
Cysteine 168 of Follistatin
Cysteine 189 of Follistatin
2b0u C 216 C 238
A redox-regulated disulphide may form within Follistatin between cysteines 245 and 267 (216 and 238 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
2b0u
Structure name
the structure of the follistatin:activin complex
Structure deposition date
2005-09-14
Thiol separation (Å)
8
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19883
Residue number A
245
Residue number B
267
Peptide name
Follistatin
Ligandability
Cysteine 245 of Follistatin
Cysteine 267 of Follistatin
2p6a C 3 C 62
A redox-regulated disulphide may form within Follistatin between cysteines 32 and 91 (3 and 62 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
2p6a
Structure name
the structure of the activin:follistatin 315 complex
Structure deposition date
2007-03-16
Thiol separation (Å)
7
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19883
Residue number A
32
Residue number B
91
Peptide name
Follistatin
Ligandability
Cysteine 32 of Follistatin
Cysteine 91 of Follistatin
2p6a D 241 D 266
A redox-regulated disulphide may form within Follistatin between cysteines 270 and 295 (241 and 266 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
2p6a
Structure name
the structure of the activin:follistatin 315 complex
Structure deposition date
2007-03-16
Thiol separation (Å)
8
Half-sphere exposure sum ?
59
Minimum pKa ?
9
% buried
24
Peptide accession
P19883
Residue number A
270
Residue number B
295
Peptide name
Follistatin
Ligandability
Cysteine 270 of Follistatin
Cysteine 295 of Follistatin
5jhw C 221 C 241
A redox-regulated disulphide may form within Follistatin between cysteines 250 and 270 (221 and 241 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
5jhw
Structure name
crystal structure of the gdf11:follistatin 288 complex
Structure deposition date
2016-04-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19883
Residue number A
250
Residue number B
270
Peptide name
Follistatin
Ligandability
Cysteine 250 of Follistatin
Cysteine 270 of Follistatin
2arp F 103 F 160
A redox-regulated disulphide may form within Follistatin between cysteines 132 and 189 (103 and 160 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
2arp
Structure name
activin a in complex with fs12 fragment of follistatin
Structure deposition date
2005-08-21
Thiol separation (Å)
8
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
P21674
Residue number A
132
Residue number B
189
Peptide name
Follistatin
Ligandability
Cysteine 132 of Follistatin
Cysteine 189 of Follistatin
3hh2 D 144 D 163
A redox-regulated disulphide may form within Follistatin between cysteines 173 and 192 (144 and 163 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
3hh2
Structure name
crystal structure of the myostatin:follistatin 288 complex
Structure deposition date
2009-05-14
Thiol separation (Å)
9
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19883
Residue number A
173
Residue number B
192
Peptide name
Follistatin
Ligandability
Cysteine 173 of Follistatin
Cysteine 192 of Follistatin
2b0u D 245 D 273
A redox-regulated disulphide may form within Follistatin between cysteines 274 and 302 (245 and 273 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
2b0u
Structure name
the structure of the follistatin:activin complex
Structure deposition date
2005-09-14
Thiol separation (Å)
9
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19883
Residue number A
274
Residue number B
302
Peptide name
Follistatin
Ligandability
Cysteine 274 of Follistatin
Cysteine 302 of Follistatin
2p6a C 26 C 59
A redox-regulated disulphide may form within Follistatin between cysteines 55 and 88 (26 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 ?
44
PDB code
2p6a
Structure name
the structure of the activin:follistatin 315 complex
Structure deposition date
2007-03-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19883
Residue number A
55
Residue number B
88
Peptide name
Follistatin
Ligandability
Cysteine 55 of Follistatin
Cysteine 88 of Follistatin
2p6a C 3 C 27
A redox-regulated disulphide may form within Follistatin between cysteines 32 and 56 (3 and 27 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
2p6a
Structure name
the structure of the activin:follistatin 315 complex
Structure deposition date
2007-03-16
Thiol separation (Å)
8
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19883
Residue number A
32
Residue number B
56
Peptide name
Follistatin
Ligandability
Cysteine 32 of Follistatin
Cysteine 56 of Follistatin
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