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Follistatin-related protein 3

Intramolecular
Cysteine 99 and cysteine 110
Cysteine 104 and cysteine 119
Cysteine 200 and cysteine 222
Cysteine 125 and cysteine 146
Cysteine 48 and cysteine 92
Cysteine 171 and cysteine 182
Cysteine 121 and cysteine 153
Cysteine 195 and cysteine 229
Cysteine 62 and cysteine 95
Cysteine 176 and cysteine 192
More...
Cysteine 135 and cysteine 167
Cysteine 211 and cysteine 243
Cysteine 38 and cysteine 61
Cysteine 61 and cysteine 62
Cysteine 61 and cysteine 95
Cysteine 104 and cysteine 110
Cysteine 176 and cysteine 182
Cysteine 110 and cysteine 119
Cysteine 171 and cysteine 176
Cysteine 182 and cysteine 192
Cysteine 38 and cysteine 95
Cysteine 99 and cysteine 104
Cysteine 38 and cysteine 62
Cysteine 99 and cysteine 119
Cysteine 171 and cysteine 192
Cysteine 61 and cysteine 92
Cysteine 135 and cysteine 192
Cysteine 92 and cysteine 95
Cysteine 125 and cysteine 153
Cysteine 176 and cysteine 195
Cysteine 48 and cysteine 61
Cysteine 62 and cysteine 92
Cysteine 38 and cysteine 92
Cysteine 121 and cysteine 146
Cysteine 104 and cysteine 121
Cysteine 119 and cysteine 121
Cysteine 48 and cysteine 95
Cysteine 176 and cysteine 229
Cysteine 104 and cysteine 153
Cysteine 121 and cysteine 125
A redox-regulated disulphide may form within Follistatin-related protein 3 between cysteines 99 and 110 (73 and 84 respectively in this structure).

Details

Redox score ?
88
PDB code
3b4v
Structure name
x-ray structure of activin in complex with fstl3
Structure deposition date
2007-10-24
Thiol separation (Å)
2
Half-sphere exposure sum ?
47
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95633
Residue number A
99
Residue number B
110
Peptide name
Follistatin-related protein 3

Ligandability

Cysteine 99 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 110 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Follistatin-related protein 3 between cysteines 104 and 119 (78 and 93 respectively in this structure).

Details

Redox score ?
88
PDB code
3sek
Structure name
crystal structure of the myostatin:follistatin-like 3 complex
Structure deposition date
2011-06-10
Thiol separation (Å)
2
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95633
Residue number A
104
Residue number B
119
Peptide name
Follistatin-related protein 3

Ligandability

Cysteine 104 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 119 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Follistatin-related protein 3 between cysteines 200 and 222 (174 and 196 respectively in this structure).

Details

Redox score ?
86
PDB code
3b4v
Structure name
x-ray structure of activin in complex with fstl3
Structure deposition date
2007-10-24
Thiol separation (Å)
2
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95633
Residue number A
200
Residue number B
222
Peptide name
Follistatin-related protein 3

Ligandability

Cysteine 200 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 222 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Follistatin-related protein 3 between cysteines 125 and 146 (99 and 120 respectively in this structure).

Details

Redox score ?
86
PDB code
3sek
Structure name
crystal structure of the myostatin:follistatin-like 3 complex
Structure deposition date
2011-06-10
Thiol separation (Å)
2
Half-sphere exposure sum ?
45
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95633
Residue number A
125
Residue number B
146
Peptide name
Follistatin-related protein 3

Ligandability

Cysteine 125 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 146 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Follistatin-related protein 3 between cysteines 48 and 92 (22 and 66 respectively in this structure).

Details

Redox score ?
86
PDB code
3b4v
Structure name
x-ray structure of activin in complex with fstl3
Structure deposition date
2007-10-24
Thiol separation (Å)
2
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95633
Residue number A
48
Residue number B
92
Peptide name
Follistatin-related protein 3

Ligandability

Cysteine 48 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 92 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Follistatin-related protein 3 between cysteines 171 and 182 (145 and 156 respectively in this structure).

Details

Redox score ?
85
PDB code
3b4v
Structure name
x-ray structure of activin in complex with fstl3
Structure deposition date
2007-10-24
Thiol separation (Å)
2
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95633
Residue number A
171
Residue number B
182
Peptide name
Follistatin-related protein 3

Ligandability

Cysteine 171 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 182 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Follistatin-related protein 3 between cysteines 121 and 153 (95 and 127 respectively in this structure).

Details

Redox score ?
85
PDB code
3sek
Structure name
crystal structure of the myostatin:follistatin-like 3 complex
Structure deposition date
2011-06-10
Thiol separation (Å)
2
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95633
Residue number A
121
Residue number B
153
Peptide name
Follistatin-related protein 3

Ligandability

Cysteine 121 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 153 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Follistatin-related protein 3 between cysteines 195 and 229 (169 and 203 respectively in this structure).

Details

Redox score ?
84
PDB code
3sek
Structure name
crystal structure of the myostatin:follistatin-like 3 complex
Structure deposition date
2011-06-10
Thiol separation (Å)
2
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95633
Residue number A
195
Residue number B
229
Peptide name
Follistatin-related protein 3

Ligandability

Cysteine 195 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 229 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Follistatin-related protein 3 between cysteines 62 and 95 (36 and 69 respectively in this structure).

Details

Redox score ?
84
PDB code
3b4v
Structure name
x-ray structure of activin in complex with fstl3
Structure deposition date
2007-10-24
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95633
Residue number A
62
Residue number B
95
Peptide name
Follistatin-related protein 3

Ligandability

Cysteine 62 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 95 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Follistatin-related protein 3 between cysteines 176 and 192 (150 and 166 respectively in this structure).

Details

Redox score ?
84
PDB code
3b4v
Structure name
x-ray structure of activin in complex with fstl3
Structure deposition date
2007-10-24
Thiol separation (Å)
2
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95633
Residue number A
176
Residue number B
192
Peptide name
Follistatin-related protein 3

Ligandability

Cysteine 176 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 192 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Follistatin-related protein 3 between cysteines 135 and 167 (109 and 141 respectively in this structure).

Details

Redox score ?
83
PDB code
3sek
Structure name
crystal structure of the myostatin:follistatin-like 3 complex
Structure deposition date
2011-06-10
Thiol separation (Å)
2
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95633
Residue number A
135
Residue number B
167
Peptide name
Follistatin-related protein 3

Ligandability

Cysteine 135 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 167 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Follistatin-related protein 3 between cysteines 211 and 243 (185 and 217 respectively in this structure).

Details

Redox score ?
83
PDB code
3b4v
Structure name
x-ray structure of activin in complex with fstl3
Structure deposition date
2007-10-24
Thiol separation (Å)
2
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95633
Residue number A
211
Residue number B
243
Peptide name
Follistatin-related protein 3

Ligandability

Cysteine 211 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 243 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Follistatin-related protein 3 between cysteines 38 and 61 (12 and 35 respectively in this structure).

Details

Redox score ?
81
PDB code
3b4v
Structure name
x-ray structure of activin in complex with fstl3
Structure deposition date
2007-10-24
Thiol separation (Å)
2
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95633
Residue number A
38
Residue number B
61
Peptide name
Follistatin-related protein 3

Ligandability

Cysteine 38 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 61 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Follistatin-related protein 3 between cysteines 61 and 62 (35 and 36 respectively in this structure).

Details

Redox score ?
72
PDB code
3b4v
Structure name
x-ray structure of activin in complex with fstl3
Structure deposition date
2007-10-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95633
Residue number A
61
Residue number B
62
Peptide name
Follistatin-related protein 3

Ligandability

Cysteine 61 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 62 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Follistatin-related protein 3 between cysteines 61 and 95 (35 and 69 respectively in this structure).

Details

Redox score ?
72
PDB code
3sek
Structure name
crystal structure of the myostatin:follistatin-like 3 complex
Structure deposition date
2011-06-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95633
Residue number A
61
Residue number B
95
Peptide name
Follistatin-related protein 3

Ligandability

Cysteine 61 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 95 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Follistatin-related protein 3 between cysteines 104 and 110 (78 and 84 respectively in this structure).

Details

Redox score ?
71
PDB code
3b4v
Structure name
x-ray structure of activin in complex with fstl3
Structure deposition date
2007-10-24
Thiol separation (Å)
5
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95633
Residue number A
104
Residue number B
110
Peptide name
Follistatin-related protein 3

Ligandability

Cysteine 104 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 110 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Follistatin-related protein 3 between cysteines 176 and 182 (150 and 156 respectively in this structure).

Details

Redox score ?
71
PDB code
3b4v
Structure name
x-ray structure of activin in complex with fstl3
Structure deposition date
2007-10-24
Thiol separation (Å)
5
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95633
Residue number A
176
Residue number B
182
Peptide name
Follistatin-related protein 3

Ligandability

Cysteine 176 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 182 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Follistatin-related protein 3 between cysteines 110 and 119 (84 and 93 respectively in this structure).

Details

Redox score ?
66
PDB code
3b4v
Structure name
x-ray structure of activin in complex with fstl3
Structure deposition date
2007-10-24
Thiol separation (Å)
6
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95633
Residue number A
110
Residue number B
119
Peptide name
Follistatin-related protein 3

Ligandability

Cysteine 110 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 119 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Follistatin-related protein 3 between cysteines 171 and 176 (145 and 150 respectively in this structure).

Details

Redox score ?
63
PDB code
3b4v
Structure name
x-ray structure of activin in complex with fstl3
Structure deposition date
2007-10-24
Thiol separation (Å)
6
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95633
Residue number A
171
Residue number B
176
Peptide name
Follistatin-related protein 3

Ligandability

Cysteine 171 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 176 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Follistatin-related protein 3 between cysteines 182 and 192 (156 and 166 respectively in this structure).

Details

Redox score ?
62
PDB code
3b4v
Structure name
x-ray structure of activin in complex with fstl3
Structure deposition date
2007-10-24
Thiol separation (Å)
5
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95633
Residue number A
182
Residue number B
192
Peptide name
Follistatin-related protein 3

Ligandability

Cysteine 182 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 192 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Follistatin-related protein 3 between cysteines 38 and 95 (12 and 69 respectively in this structure).

Details

Redox score ?
62
PDB code
3b4v
Structure name
x-ray structure of activin in complex with fstl3
Structure deposition date
2007-10-24
Thiol separation (Å)
5
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95633
Residue number A
38
Residue number B
95
Peptide name
Follistatin-related protein 3

Ligandability

Cysteine 38 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 95 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Follistatin-related protein 3 between cysteines 99 and 104 (73 and 78 respectively in this structure).

Details

Redox score ?
61
PDB code
3b4v
Structure name
x-ray structure of activin in complex with fstl3
Structure deposition date
2007-10-24
Thiol separation (Å)
7
Half-sphere exposure sum ?
46
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95633
Residue number A
99
Residue number B
104
Peptide name
Follistatin-related protein 3

Ligandability

Cysteine 99 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 104 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Follistatin-related protein 3 between cysteines 38 and 62 (12 and 36 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
3b4v
Structure name
x-ray structure of activin in complex with fstl3
Structure deposition date
2007-10-24
Thiol separation (Å)
6
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95633
Residue number A
38
Residue number B
62
Peptide name
Follistatin-related protein 3

Ligandability

Cysteine 38 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 62 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Follistatin-related protein 3 between cysteines 99 and 119 (73 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 ?
57
PDB code
3b4v
Structure name
x-ray structure of activin in complex with fstl3
Structure deposition date
2007-10-24
Thiol separation (Å)
7
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95633
Residue number A
99
Residue number B
119
Peptide name
Follistatin-related protein 3

Ligandability

Cysteine 99 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 119 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Follistatin-related protein 3 between cysteines 171 and 192 (145 and 166 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
3b4v
Structure name
x-ray structure of activin in complex with fstl3
Structure deposition date
2007-10-24
Thiol separation (Å)
7
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95633
Residue number A
171
Residue number B
192
Peptide name
Follistatin-related protein 3

Ligandability

Cysteine 171 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 192 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Follistatin-related protein 3 between cysteines 61 and 92 (35 and 66 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
3b4v
Structure name
x-ray structure of activin in complex with fstl3
Structure deposition date
2007-10-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95633
Residue number A
61
Residue number B
92
Peptide name
Follistatin-related protein 3

Ligandability

Cysteine 61 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 92 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Follistatin-related protein 3 between cysteines 135 and 192 (109 and 166 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
3sek
Structure name
crystal structure of the myostatin:follistatin-like 3 complex
Structure deposition date
2011-06-10
Thiol separation (Å)
8
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95633
Residue number A
135
Residue number B
192
Peptide name
Follistatin-related protein 3

Ligandability

Cysteine 135 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 192 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Follistatin-related protein 3 between cysteines 92 and 95 (66 and 69 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
3b4v
Structure name
x-ray structure of activin in complex with fstl3
Structure deposition date
2007-10-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95633
Residue number A
92
Residue number B
95
Peptide name
Follistatin-related protein 3

Ligandability

Cysteine 92 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 95 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Follistatin-related protein 3 between cysteines 125 and 153 (30 and 58 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
2kcx
Structure name
solution nmr structure of kazal-1 domain of human follistatin-related protein 3 (fstl-3)
Structure deposition date
2008-12-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95633
Residue number A
125
Residue number B
153
Peptide name
Follistatin-related protein 3

Ligandability

Cysteine 125 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 153 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Follistatin-related protein 3 between cysteines 176 and 195 (150 and 169 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
3b4v
Structure name
x-ray structure of activin in complex with fstl3
Structure deposition date
2007-10-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95633
Residue number A
176
Residue number B
195
Peptide name
Follistatin-related protein 3

Ligandability

Cysteine 176 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 195 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Follistatin-related protein 3 between cysteines 48 and 61 (22 and 35 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
3b4v
Structure name
x-ray structure of activin in complex with fstl3
Structure deposition date
2007-10-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95633
Residue number A
48
Residue number B
61
Peptide name
Follistatin-related protein 3

Ligandability

Cysteine 48 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 61 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Follistatin-related protein 3 between cysteines 62 and 92 (36 and 66 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
3b4v
Structure name
x-ray structure of activin in complex with fstl3
Structure deposition date
2007-10-24
Thiol separation (Å)
10
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95633
Residue number A
62
Residue number B
92
Peptide name
Follistatin-related protein 3

Ligandability

Cysteine 62 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 92 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Follistatin-related protein 3 between cysteines 38 and 92 (12 and 66 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
3b4v
Structure name
x-ray structure of activin in complex with fstl3
Structure deposition date
2007-10-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95633
Residue number A
38
Residue number B
92
Peptide name
Follistatin-related protein 3

Ligandability

Cysteine 38 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 92 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Follistatin-related protein 3 between cysteines 121 and 146 (26 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 ?
42
PDB code
2kcx
Structure name
solution nmr structure of kazal-1 domain of human follistatin-related protein 3 (fstl-3)
Structure deposition date
2008-12-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95633
Residue number A
121
Residue number B
146
Peptide name
Follistatin-related protein 3

Ligandability

Cysteine 121 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 146 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Follistatin-related protein 3 between cysteines 104 and 121 (78 and 95 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
3b4v
Structure name
x-ray structure of activin in complex with fstl3
Structure deposition date
2007-10-24
Thiol separation (Å)
10
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95633
Residue number A
104
Residue number B
121
Peptide name
Follistatin-related protein 3

Ligandability

Cysteine 104 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 121 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Follistatin-related protein 3 between cysteines 119 and 121 (93 and 95 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
3b4v
Structure name
x-ray structure of activin in complex with fstl3
Structure deposition date
2007-10-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95633
Residue number A
119
Residue number B
121
Peptide name
Follistatin-related protein 3

Ligandability

Cysteine 119 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 121 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Follistatin-related protein 3 between cysteines 48 and 95 (22 and 69 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
3b4v
Structure name
x-ray structure of activin in complex with fstl3
Structure deposition date
2007-10-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95633
Residue number A
48
Residue number B
95
Peptide name
Follistatin-related protein 3

Ligandability

Cysteine 48 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 95 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Follistatin-related protein 3 between cysteines 176 and 229 (150 and 203 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
3b4v
Structure name
x-ray structure of activin in complex with fstl3
Structure deposition date
2007-10-24
Thiol separation (Å)
10
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95633
Residue number A
176
Residue number B
229
Peptide name
Follistatin-related protein 3

Ligandability

Cysteine 176 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 229 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Follistatin-related protein 3 between cysteines 104 and 153 (78 and 127 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
3b4v
Structure name
x-ray structure of activin in complex with fstl3
Structure deposition date
2007-10-24
Thiol separation (Å)
10
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95633
Residue number A
104
Residue number B
153
Peptide name
Follistatin-related protein 3

Ligandability

Cysteine 104 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 153 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Follistatin-related protein 3 between cysteines 121 and 125 (26 and 30 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
2kcx
Structure name
solution nmr structure of kazal-1 domain of human follistatin-related protein 3 (fstl-3)
Structure deposition date
2008-12-30
Thiol separation (Å)
10
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95633
Residue number A
121
Residue number B
125
Peptide name
Follistatin-related protein 3

Ligandability

Cysteine 121 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 125 of Follistatin-related protein 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

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