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a tool for identifying drug-targetable redox-active disulphides

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Growth/differentiation factor 8

Intermolecular
Cysteine 339 and cysteine 339
Cysteine 340 and cysteine 341
Cysteine 313 and cysteine 339
Cysteine 340 and cysteine 310
Intramolecular
Cysteine 313 and cysteine 374
Cysteine 281 and cysteine 340
Cysteine 309 and cysteine 372
Cysteine 273 and cysteine 283
Cysteine 282 and cysteine 375
Cysteine 281 and cysteine 313
More...
Cysteine 341 and cysteine 373
Cysteine 314 and cysteine 341
Cysteine 310 and cysteine 341
Cysteine 282 and cysteine 373
Cysteine 137 and cysteine 138
Cysteine 282 and cysteine 310
Cysteine 341 and cysteine 375
Cysteine 314 and cysteine 340
Cysteine 272 and cysteine 309
Cysteine 283 and cysteine 373
Cysteine 282 and cysteine 283
Cysteine 272 and cysteine 372
Cysteine 283 and cysteine 341
Cysteine 273 and cysteine 341
Cysteine 272 and cysteine 281
Cysteine 309 and cysteine 313
Cysteine 309 and cysteine 374
Cysteine 309 and cysteine 339
Cysteine 340 and cysteine 375
Cysteine 314 and cysteine 373
Cysteine 282 and cysteine 340
Cysteine 283 and cysteine 310
Cysteine 373 and cysteine 375
A redox-regulated disulphide may form between two units of Growth/differentiation factor 8 at cysteines 339 and 339 (73 and 73 respectively in this structure).

Details

Redox score ?
81
PDB code
5f3h
Structure name
structure of myostatin in complex with humanized rk35 antibody
Structure deposition date
2015-12-02
Thiol separation (Å)
2
Half-sphere exposure sum ?
85
Minimum pKa ?
nan
% buried
nan
Peptide A name
Growth/differentiation factor 8
Peptide B name
Growth/differentiation factor 8
Peptide A accession
O14793
Peptide B accession
O14793
Peptide A residue number
339
Peptide B residue number
339

Ligandability

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 between two units of Growth/differentiation factor 8 at cysteines 340 and 341 (73 and 74 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
5ji1
Structure name
crystal structure of gdf8
Structure deposition date
2016-04-21
Thiol separation (Å)
8
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide A name
Growth/differentiation factor 8
Peptide B name
Growth/differentiation factor 8
Peptide A accession
O08689
Peptide B accession
O08689
Peptide A residue number
340
Peptide B residue number
341

Ligandability

Cysteine 340 of Growth/differentiation factor 8

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 341 of Growth/differentiation factor 8

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 between two units of Growth/differentiation factor 8 at cysteines 313 and 339 (47 and 73 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
5f3b
Structure name
structure of myostatin in complex with chimeric rk35 antibody
Structure deposition date
2015-12-02
Thiol separation (Å)
9
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide A name
Growth/differentiation factor 8
Peptide B name
Growth/differentiation factor 8
Peptide A accession
O14793
Peptide B accession
O14793
Peptide A residue number
313
Peptide B residue number
339

Ligandability

Cysteine 313 of Growth/differentiation factor 8

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 339 of Growth/differentiation factor 8

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 between two units of Growth/differentiation factor 8 at cysteines 340 and 310 (73 and 43 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
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 ?
89
Minimum pKa ?
nan
% buried
nan
Peptide A name
Growth/differentiation factor 8
Peptide B name
Growth/differentiation factor 8
Peptide A accession
O08689
Peptide B accession
O08689
Peptide A residue number
340
Peptide B residue number
310

Ligandability

Cysteine 340 of Growth/differentiation factor 8

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 310 of Growth/differentiation factor 8

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 Growth/differentiation factor 8 between cysteines 313 and 374 (47 and 108 respectively in this structure).

Details

Redox score ?
85
PDB code
5f3b
Structure name
structure of myostatin in complex with chimeric rk35 antibody
Structure deposition date
2015-12-02
Thiol separation (Å)
2
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
O14793
Residue number A
313
Residue number B
374
Peptide name
Growth/differentiation factor 8

Ligandability

Cysteine 313 of Growth/differentiation factor 8

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 374 of Growth/differentiation factor 8

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 Growth/differentiation factor 8 between cysteines 281 and 340.

Details

Redox score ?
84
PDB code
5ntu
Structure name
crystal structure of human pro-myostatin precursor at 2
Structure deposition date
2017-04-28
Thiol separation (Å)
2
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
O14793
Residue number A
281
Residue number B
340
Peptide name
Growth/differentiation factor 8

Ligandability

Cysteine 281 of Growth/differentiation factor 8

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 340 of Growth/differentiation factor 8

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 Growth/differentiation factor 8 between cysteines 309 and 372 (43 and 106 respectively in this structure).

Details

Redox score ?
83
PDB code
5f3h
Structure name
structure of myostatin in complex with humanized rk35 antibody
Structure deposition date
2015-12-02
Thiol separation (Å)
2
Half-sphere exposure sum ?
85
Minimum pKa ?
nan
% buried
nan
Peptide accession
O14793
Residue number A
309
Residue number B
372
Peptide name
Growth/differentiation factor 8

Ligandability

Cysteine 309 of Growth/differentiation factor 8

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 372 of Growth/differentiation factor 8

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 Growth/differentiation factor 8 between cysteines 273 and 283 (6 and 16 respectively in this structure).

Details

Redox score ?
80
PDB code
5ji1
Structure name
crystal structure of gdf8
Structure deposition date
2016-04-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
O08689
Residue number A
273
Residue number B
283
Peptide name
Growth/differentiation factor 8

Ligandability

Cysteine 273 of Growth/differentiation factor 8

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 283 of Growth/differentiation factor 8

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 Growth/differentiation factor 8 between cysteines 282 and 375 (15 and 108 respectively in this structure).

Details

Redox score ?
71
PDB code
5ji1
Structure name
crystal structure of gdf8
Structure deposition date
2016-04-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
O08689
Residue number A
282
Residue number B
375
Peptide name
Growth/differentiation factor 8

Ligandability

Cysteine 282 of Growth/differentiation factor 8

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 375 of Growth/differentiation factor 8

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 Growth/differentiation factor 8 between cysteines 281 and 313.

Details

Redox score ?
70
PDB code
5ntu
Structure name
crystal structure of human pro-myostatin precursor at 2
Structure deposition date
2017-04-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
O14793
Residue number A
281
Residue number B
313
Peptide name
Growth/differentiation factor 8

Ligandability

Cysteine 281 of Growth/differentiation factor 8

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 313 of Growth/differentiation factor 8

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 Growth/differentiation factor 8 between cysteines 341 and 373 (74 and 106 respectively in this structure).

Details

Redox score ?
67
PDB code
5ji1
Structure name
crystal structure of gdf8
Structure deposition date
2016-04-21
Thiol separation (Å)
5
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
O08689
Residue number A
341
Residue number B
373
Peptide name
Growth/differentiation factor 8

Ligandability

Cysteine 341 of Growth/differentiation factor 8

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 373 of Growth/differentiation factor 8

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 Growth/differentiation factor 8 between cysteines 314 and 341 (47 and 74 respectively in this structure).

Details

Redox score ?
67
PDB code
5ji1
Structure name
crystal structure of gdf8
Structure deposition date
2016-04-21
Thiol separation (Å)
5
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
O08689
Residue number A
314
Residue number B
341
Peptide name
Growth/differentiation factor 8

Ligandability

Cysteine 314 of Growth/differentiation factor 8

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 341 of Growth/differentiation factor 8

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 Growth/differentiation factor 8 between cysteines 310 and 341 (43 and 74 respectively in this structure).

Details

Redox score ?
66
PDB code
5ji1
Structure name
crystal structure of gdf8
Structure deposition date
2016-04-21
Thiol separation (Å)
5
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
O08689
Residue number A
310
Residue number B
341
Peptide name
Growth/differentiation factor 8

Ligandability

Cysteine 310 of Growth/differentiation factor 8

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 341 of Growth/differentiation factor 8

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 Growth/differentiation factor 8 between cysteines 282 and 373 (15 and 106 respectively in this structure).

Details

Redox score ?
66
PDB code
5ji1
Structure name
crystal structure of gdf8
Structure deposition date
2016-04-21
Thiol separation (Å)
5
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
O08689
Residue number A
282
Residue number B
373
Peptide name
Growth/differentiation factor 8

Ligandability

Cysteine 282 of Growth/differentiation factor 8

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 373 of Growth/differentiation factor 8

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 Growth/differentiation factor 8 between cysteines 137 and 138.

Details

Redox score ?
64
PDB code
6umx
Structure name
structural basis for specific inhibition of extracellular activation of pro/latent myostatin by srk-015
Structure deposition date
2019-10-10
Thiol separation (Å)
6
Half-sphere exposure sum ?
57
Minimum pKa ?
10
% buried
54
Peptide accession
O14793
Residue number A
137
Residue number B
138
Peptide name
Growth/differentiation factor 8

Ligandability

Cysteine 137 of Growth/differentiation factor 8

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 138 of Growth/differentiation factor 8

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 Growth/differentiation factor 8 between cysteines 282 and 310 (15 and 43 respectively in this structure).

Details

Redox score ?
63
PDB code
5ji1
Structure name
crystal structure of gdf8
Structure deposition date
2016-04-21
Thiol separation (Å)
6
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
O08689
Residue number A
282
Residue number B
310
Peptide name
Growth/differentiation factor 8

Ligandability

Cysteine 282 of Growth/differentiation factor 8

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 310 of Growth/differentiation factor 8

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 Growth/differentiation factor 8 between cysteines 341 and 375 (74 and 108 respectively in this structure).

Details

Redox score ?
61
PDB code
5ji1
Structure name
crystal structure of gdf8
Structure deposition date
2016-04-21
Thiol separation (Å)
6
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
O08689
Residue number A
341
Residue number B
375
Peptide name
Growth/differentiation factor 8

Ligandability

Cysteine 341 of Growth/differentiation factor 8

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 375 of Growth/differentiation factor 8

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 Growth/differentiation factor 8 between cysteines 314 and 340 (47 and 73 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
5ji1
Structure name
crystal structure of gdf8
Structure deposition date
2016-04-21
Thiol separation (Å)
6
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
O08689
Residue number A
314
Residue number B
340
Peptide name
Growth/differentiation factor 8

Ligandability

Cysteine 314 of Growth/differentiation factor 8

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 340 of Growth/differentiation factor 8

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 Growth/differentiation factor 8 between cysteines 272 and 309. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
5nxs
Structure name
crystal structure of human pro-myostatin precursor at 4
Structure deposition date
2017-05-10
Thiol separation (Å)
8
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
O14793
Residue number A
272
Residue number B
309
Peptide name
Growth/differentiation factor 8

Ligandability

Cysteine 272 of Growth/differentiation factor 8

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 309 of Growth/differentiation factor 8

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 Growth/differentiation factor 8 between cysteines 283 and 373 (16 and 106 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
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 ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
O08689
Residue number A
283
Residue number B
373
Peptide name
Growth/differentiation factor 8

Ligandability

Cysteine 283 of Growth/differentiation factor 8

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 373 of Growth/differentiation factor 8

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 Growth/differentiation factor 8 between cysteines 282 and 283 (15 and 16 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
3sek
Structure name
crystal structure of the myostatin:follistatin-like 3 complex
Structure deposition date
2011-06-10
Thiol separation (Å)
7
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
O08689
Residue number A
282
Residue number B
283
Peptide name
Growth/differentiation factor 8

Ligandability

Cysteine 282 of Growth/differentiation factor 8

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 283 of Growth/differentiation factor 8

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 Growth/differentiation factor 8 between cysteines 272 and 372. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
5ntu
Structure name
crystal structure of human pro-myostatin precursor at 2
Structure deposition date
2017-04-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
O14793
Residue number A
272
Residue number B
372
Peptide name
Growth/differentiation factor 8

Ligandability

Cysteine 272 of Growth/differentiation factor 8

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 372 of Growth/differentiation factor 8

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 Growth/differentiation factor 8 between cysteines 283 and 341 (16 and 74 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)
8
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
O08689
Residue number A
283
Residue number B
341
Peptide name
Growth/differentiation factor 8

Ligandability

Cysteine 283 of Growth/differentiation factor 8

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 341 of Growth/differentiation factor 8

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 Growth/differentiation factor 8 between cysteines 273 and 341 (6 and 74 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
5ji1
Structure name
crystal structure of gdf8
Structure deposition date
2016-04-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
O08689
Residue number A
273
Residue number B
341
Peptide name
Growth/differentiation factor 8

Ligandability

Cysteine 273 of Growth/differentiation factor 8

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 341 of Growth/differentiation factor 8

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 Growth/differentiation factor 8 between cysteines 272 and 281. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
5ntu
Structure name
crystal structure of human pro-myostatin precursor at 2
Structure deposition date
2017-04-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
O14793
Residue number A
272
Residue number B
281
Peptide name
Growth/differentiation factor 8

Ligandability

Cysteine 272 of Growth/differentiation factor 8

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 281 of Growth/differentiation factor 8

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 Growth/differentiation factor 8 between cysteines 309 and 313 (43 and 47 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
5f3h
Structure name
structure of myostatin in complex with humanized rk35 antibody
Structure deposition date
2015-12-02
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
O14793
Residue number A
309
Residue number B
313
Peptide name
Growth/differentiation factor 8

Ligandability

Cysteine 309 of Growth/differentiation factor 8

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 313 of Growth/differentiation factor 8

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 Growth/differentiation factor 8 between cysteines 309 and 374. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
5nxs
Structure name
crystal structure of human pro-myostatin precursor at 4
Structure deposition date
2017-05-10
Thiol separation (Å)
9
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
O14793
Residue number A
309
Residue number B
374
Peptide name
Growth/differentiation factor 8

Ligandability

Cysteine 309 of Growth/differentiation factor 8

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 374 of Growth/differentiation factor 8

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 Growth/differentiation factor 8 between cysteines 309 and 339 (43 and 73 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
5f3h
Structure name
structure of myostatin in complex with humanized rk35 antibody
Structure deposition date
2015-12-02
Thiol separation (Å)
9
Half-sphere exposure sum ?
90
Minimum pKa ?
nan
% buried
nan
Peptide accession
O14793
Residue number A
309
Residue number B
339
Peptide name
Growth/differentiation factor 8

Ligandability

Cysteine 309 of Growth/differentiation factor 8

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 339 of Growth/differentiation factor 8

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 Growth/differentiation factor 8 between cysteines 340 and 375 (73 and 108 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
3hh2
Structure name
crystal structure of the myostatin:follistatin 288 complex
Structure deposition date
2009-05-14
Thiol separation (Å)
8
Half-sphere exposure sum ?
83
Minimum pKa ?
nan
% buried
nan
Peptide accession
O08689
Residue number A
340
Residue number B
375
Peptide name
Growth/differentiation factor 8

Ligandability

Cysteine 340 of Growth/differentiation factor 8

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 375 of Growth/differentiation factor 8

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 Growth/differentiation factor 8 between cysteines 314 and 373 (47 and 106 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
3hh2
Structure name
crystal structure of the myostatin:follistatin 288 complex
Structure deposition date
2009-05-14
Thiol separation (Å)
10
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
O08689
Residue number A
314
Residue number B
373
Peptide name
Growth/differentiation factor 8

Ligandability

Cysteine 314 of Growth/differentiation factor 8

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 373 of Growth/differentiation factor 8

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 Growth/differentiation factor 8 between cysteines 282 and 340 (15 and 73 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
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 ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
O08689
Residue number A
282
Residue number B
340
Peptide name
Growth/differentiation factor 8

Ligandability

Cysteine 282 of Growth/differentiation factor 8

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 340 of Growth/differentiation factor 8

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 Growth/differentiation factor 8 between cysteines 283 and 310 (16 and 43 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
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 ?
87
Minimum pKa ?
nan
% buried
nan
Peptide accession
O08689
Residue number A
283
Residue number B
310
Peptide name
Growth/differentiation factor 8

Ligandability

Cysteine 283 of Growth/differentiation factor 8

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 310 of Growth/differentiation factor 8

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 Growth/differentiation factor 8 between cysteines 373 and 375 (106 and 108 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
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 ?
82
Minimum pKa ?
nan
% buried
nan
Peptide accession
O08689
Residue number A
373
Residue number B
375
Peptide name
Growth/differentiation factor 8

Ligandability

Cysteine 373 of Growth/differentiation factor 8

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 375 of Growth/differentiation factor 8

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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