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Growth/differentiation factor 11

Intermolecular
Cysteine 371 and cysteine 371
Cysteine 372 and cysteine 371
Cysteine 341 and cysteine 371
Intramolecular
Cysteine 313 and cysteine 372
Cysteine 345 and cysteine 406
Cysteine 341 and cysteine 404
Cysteine 304 and cysteine 314
Cysteine 313 and cysteine 345
Cysteine 345 and cysteine 372
Cysteine 341 and cysteine 372
More...
Cysteine 372 and cysteine 404
Cysteine 313 and cysteine 406
Cysteine 313 and cysteine 404
Cysteine 372 and cysteine 406
Cysteine 313 and cysteine 341
Cysteine 345 and cysteine 371
Cysteine 314 and cysteine 404
Cysteine 314 and cysteine 372
Cysteine 313 and cysteine 314
Cysteine 341 and cysteine 345
Cysteine 345 and cysteine 404
Cysteine 404 and cysteine 406
Cysteine 304 and cysteine 313
Cysteine 304 and cysteine 404
Cysteine 314 and cysteine 341
Cysteine 371 and cysteine 406
Cysteine 313 and cysteine 371
Cysteine 304 and cysteine 372
Cysteine 304 and cysteine 341
Cysteine 341 and cysteine 406
Cysteine 371 and cysteine 404
A redox-regulated disulphide may form between two units of Growth/differentiation factor 11 at cysteines 371 and 371 (73 and 73 respectively in this structure).

Details

Redox score ?
77
PDB code
5jhw
Structure name
crystal structure of the gdf11:follistatin 288 complex
Structure deposition date
2016-04-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide A name
Growth/differentiation factor 11
Peptide B name
Growth/differentiation factor 11
Peptide A accession
O95390
Peptide B accession
O95390
Peptide A residue number
371
Peptide B residue number
371

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 11 at cysteines 372 and 371 (74 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 ?
42
PDB code
5jhw
Structure name
crystal structure of the gdf11:follistatin 288 complex
Structure deposition date
2016-04-21
Thiol separation (Å)
8
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide A name
Growth/differentiation factor 11
Peptide B name
Growth/differentiation factor 11
Peptide A accession
O95390
Peptide B accession
O95390
Peptide A residue number
372
Peptide B residue number
371

Ligandability

Cysteine 372 of Growth/differentiation factor 11

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 371 of Growth/differentiation factor 11

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 11 at cysteines 341 and 371 (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 ?
40
PDB code
5jhw
Structure name
crystal structure of the gdf11:follistatin 288 complex
Structure deposition date
2016-04-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
87
Minimum pKa ?
nan
% buried
nan
Peptide A name
Growth/differentiation factor 11
Peptide B name
Growth/differentiation factor 11
Peptide A accession
O95390
Peptide B accession
O95390
Peptide A residue number
341
Peptide B residue number
371

Ligandability

Cysteine 341 of Growth/differentiation factor 11

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 371 of Growth/differentiation factor 11

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 11 between cysteines 313 and 372.

Details

Redox score ?
86
PDB code
7mrz
Structure name
structure of gdf11 bound to fused actriib-ecd and alk4-ecd with anti- actriib fab fragment
Structure deposition date
2021-05-10
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95390
Residue number A
313
Residue number B
372
Peptide name
Growth/differentiation factor 11

Ligandability

Cysteine 313 of Growth/differentiation factor 11

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 11

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 11 between cysteines 345 and 406 (47 and 108 respectively in this structure).

Details

Redox score ?
84
PDB code
5jhw
Structure name
crystal structure of the gdf11:follistatin 288 complex
Structure deposition date
2016-04-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95390
Residue number A
345
Residue number B
406
Peptide name
Growth/differentiation factor 11

Ligandability

Cysteine 345 of Growth/differentiation factor 11

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 406 of Growth/differentiation factor 11

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 11 between cysteines 341 and 404 (43 and 106 respectively in this structure).

Details

Redox score ?
82
PDB code
5jhw
Structure name
crystal structure of the gdf11:follistatin 288 complex
Structure deposition date
2016-04-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
84
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95390
Residue number A
341
Residue number B
404
Peptide name
Growth/differentiation factor 11

Ligandability

Cysteine 341 of Growth/differentiation factor 11

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 404 of Growth/differentiation factor 11

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 11 between cysteines 304 and 314 (6 and 16 respectively in this structure).

Details

Redox score ?
80
PDB code
5uhm
Structure name
apo-structure of mature growth differentiation factor 11
Structure deposition date
2017-01-11
Thiol separation (Å)
2
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95390
Residue number A
304
Residue number B
314
Peptide name
Growth/differentiation factor 11

Ligandability

Cysteine 304 of Growth/differentiation factor 11

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 314 of Growth/differentiation factor 11

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 11 between cysteines 313 and 345 (15 and 47 respectively in this structure).

Details

Redox score ?
74
PDB code
6mac
Structure name
ternary structure of gdf11 bound to actriib-ecd and alk5-ecd
Structure deposition date
2018-08-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95390
Residue number A
313
Residue number B
345
Peptide name
Growth/differentiation factor 11

Ligandability

Cysteine 313 of Growth/differentiation factor 11

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 345 of Growth/differentiation factor 11

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 11 between cysteines 345 and 372 (47 and 74 respectively in this structure).

Details

Redox score ?
72
PDB code
5uhm
Structure name
apo-structure of mature growth differentiation factor 11
Structure deposition date
2017-01-11
Thiol separation (Å)
5
Half-sphere exposure sum ?
45
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95390
Residue number A
345
Residue number B
372
Peptide name
Growth/differentiation factor 11

Ligandability

Cysteine 345 of Growth/differentiation factor 11

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 11

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 11 between cysteines 341 and 372.

Details

Redox score ?
72
PDB code
7mrz
Structure name
structure of gdf11 bound to fused actriib-ecd and alk4-ecd with anti- actriib fab fragment
Structure deposition date
2021-05-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95390
Residue number A
341
Residue number B
372
Peptide name
Growth/differentiation factor 11

Ligandability

Cysteine 341 of Growth/differentiation factor 11

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 11

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 11 between cysteines 372 and 404.

Details

Redox score ?
71
PDB code
7mrz
Structure name
structure of gdf11 bound to fused actriib-ecd and alk4-ecd with anti- actriib fab fragment
Structure deposition date
2021-05-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95390
Residue number A
372
Residue number B
404
Peptide name
Growth/differentiation factor 11

Ligandability

Cysteine 372 of Growth/differentiation factor 11

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 404 of Growth/differentiation factor 11

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 11 between cysteines 313 and 406 (15 and 108 respectively in this structure).

Details

Redox score ?
70
PDB code
6mac
Structure name
ternary structure of gdf11 bound to actriib-ecd and alk5-ecd
Structure deposition date
2018-08-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95390
Residue number A
313
Residue number B
406
Peptide name
Growth/differentiation factor 11

Ligandability

Cysteine 313 of Growth/differentiation factor 11

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 406 of Growth/differentiation factor 11

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 11 between cysteines 313 and 404.

Details

Redox score ?
66
PDB code
7mrz
Structure name
structure of gdf11 bound to fused actriib-ecd and alk4-ecd with anti- actriib fab fragment
Structure deposition date
2021-05-10
Thiol separation (Å)
5
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95390
Residue number A
313
Residue number B
404
Peptide name
Growth/differentiation factor 11

Ligandability

Cysteine 313 of Growth/differentiation factor 11

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 404 of Growth/differentiation factor 11

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 11 between cysteines 372 and 406 (74 and 108 respectively in this structure).

Details

Redox score ?
66
PDB code
5uhm
Structure name
apo-structure of mature growth differentiation factor 11
Structure deposition date
2017-01-11
Thiol separation (Å)
6
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95390
Residue number A
372
Residue number B
406
Peptide name
Growth/differentiation factor 11

Ligandability

Cysteine 372 of Growth/differentiation factor 11

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 406 of Growth/differentiation factor 11

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 11 between cysteines 313 and 341 (15 and 43 respectively in this structure).

Details

Redox score ?
63
PDB code
5uhm
Structure name
apo-structure of mature growth differentiation factor 11
Structure deposition date
2017-01-11
Thiol separation (Å)
6
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95390
Residue number A
313
Residue number B
341
Peptide name
Growth/differentiation factor 11

Ligandability

Cysteine 313 of Growth/differentiation factor 11

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 11

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 11 between cysteines 345 and 371 (47 and 73 respectively in this structure).

Details

Redox score ?
60
PDB code
5uhm
Structure name
apo-structure of mature growth differentiation factor 11
Structure deposition date
2017-01-11
Thiol separation (Å)
7
Half-sphere exposure sum ?
37
Minimum pKa ?
10
% buried
nan
Peptide accession
O95390
Residue number A
345
Residue number B
371
Peptide name
Growth/differentiation factor 11

Ligandability

Cysteine 345 of Growth/differentiation factor 11

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 371 of Growth/differentiation factor 11

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 11 between cysteines 314 and 404. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
7mrz
Structure name
structure of gdf11 bound to fused actriib-ecd and alk4-ecd with anti- actriib fab fragment
Structure deposition date
2021-05-10
Thiol separation (Å)
6
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95390
Residue number A
314
Residue number B
404
Peptide name
Growth/differentiation factor 11

Ligandability

Cysteine 314 of Growth/differentiation factor 11

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 404 of Growth/differentiation factor 11

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 11 between cysteines 314 and 372 (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 ?
51
PDB code
5uhm
Structure name
apo-structure of mature growth differentiation factor 11
Structure deposition date
2017-01-11
Thiol separation (Å)
8
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95390
Residue number A
314
Residue number B
372
Peptide name
Growth/differentiation factor 11

Ligandability

Cysteine 314 of Growth/differentiation factor 11

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 11

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 11 between cysteines 313 and 314 (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 ?
48
PDB code
5jhw
Structure name
crystal structure of the gdf11:follistatin 288 complex
Structure deposition date
2016-04-21
Thiol separation (Å)
7
Half-sphere exposure sum ?
83
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95390
Residue number A
313
Residue number B
314
Peptide name
Growth/differentiation factor 11

Ligandability

Cysteine 313 of Growth/differentiation factor 11

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 314 of Growth/differentiation factor 11

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 11 between cysteines 341 and 345 (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 ?
46
PDB code
6mac
Structure name
ternary structure of gdf11 bound to actriib-ecd and alk5-ecd
Structure deposition date
2018-08-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95390
Residue number A
341
Residue number B
345
Peptide name
Growth/differentiation factor 11

Ligandability

Cysteine 341 of Growth/differentiation factor 11

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 345 of Growth/differentiation factor 11

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 11 between cysteines 345 and 404 (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 ?
44
PDB code
5uhm
Structure name
apo-structure of mature growth differentiation factor 11
Structure deposition date
2017-01-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95390
Residue number A
345
Residue number B
404
Peptide name
Growth/differentiation factor 11

Ligandability

Cysteine 345 of Growth/differentiation factor 11

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 404 of Growth/differentiation factor 11

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 11 between cysteines 404 and 406. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
7mrz
Structure name
structure of gdf11 bound to fused actriib-ecd and alk4-ecd with anti- actriib fab fragment
Structure deposition date
2021-05-10
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95390
Residue number A
404
Residue number B
406
Peptide name
Growth/differentiation factor 11

Ligandability

Cysteine 404 of Growth/differentiation factor 11

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 406 of Growth/differentiation factor 11

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 11 between cysteines 304 and 313 (6 and 15 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
5jhw
Structure name
crystal structure of the gdf11:follistatin 288 complex
Structure deposition date
2016-04-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95390
Residue number A
304
Residue number B
313
Peptide name
Growth/differentiation factor 11

Ligandability

Cysteine 304 of Growth/differentiation factor 11

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 11

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 11 between cysteines 304 and 404 (6 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 ?
43
PDB code
5uhm
Structure name
apo-structure of mature growth differentiation factor 11
Structure deposition date
2017-01-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95390
Residue number A
304
Residue number B
404
Peptide name
Growth/differentiation factor 11

Ligandability

Cysteine 304 of Growth/differentiation factor 11

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 404 of Growth/differentiation factor 11

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 11 between cysteines 314 and 341 (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 ?
42
PDB code
5e4g
Structure name
crystal structure of human growth differentiation factor 11 (gdf-11)
Structure deposition date
2015-10-06
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95390
Residue number A
314
Residue number B
341
Peptide name
Growth/differentiation factor 11

Ligandability

Cysteine 314 of Growth/differentiation factor 11

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 11

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 11 between cysteines 371 and 406. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
7mrz
Structure name
structure of gdf11 bound to fused actriib-ecd and alk4-ecd with anti- actriib fab fragment
Structure deposition date
2021-05-10
Thiol separation (Å)
9
Half-sphere exposure sum ?
61
Minimum pKa ?
9
% buried
nan
Peptide accession
O95390
Residue number A
371
Residue number B
406
Peptide name
Growth/differentiation factor 11

Ligandability

Cysteine 371 of Growth/differentiation factor 11

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 406 of Growth/differentiation factor 11

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 11 between cysteines 313 and 371 (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 ?
42
PDB code
5e4g
Structure name
crystal structure of human growth differentiation factor 11 (gdf-11)
Structure deposition date
2015-10-06
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
9
% buried
nan
Peptide accession
O95390
Residue number A
313
Residue number B
371
Peptide name
Growth/differentiation factor 11

Ligandability

Cysteine 313 of Growth/differentiation factor 11

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 371 of Growth/differentiation factor 11

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 11 between cysteines 304 and 372 (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 ?
42
PDB code
5jhw
Structure name
crystal structure of the gdf11:follistatin 288 complex
Structure deposition date
2016-04-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95390
Residue number A
304
Residue number B
372
Peptide name
Growth/differentiation factor 11

Ligandability

Cysteine 304 of Growth/differentiation factor 11

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 11

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 11 between cysteines 304 and 341. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
7mrz
Structure name
structure of gdf11 bound to fused actriib-ecd and alk4-ecd with anti- actriib fab fragment
Structure deposition date
2021-05-10
Thiol separation (Å)
10
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95390
Residue number A
304
Residue number B
341
Peptide name
Growth/differentiation factor 11

Ligandability

Cysteine 304 of Growth/differentiation factor 11

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 11

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 11 between cysteines 341 and 406 (43 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 ?
36
PDB code
5jhw
Structure name
crystal structure of the gdf11:follistatin 288 complex
Structure deposition date
2016-04-21
Thiol separation (Å)
10
Half-sphere exposure sum ?
92
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95390
Residue number A
341
Residue number B
406
Peptide name
Growth/differentiation factor 11

Ligandability

Cysteine 341 of Growth/differentiation factor 11

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 406 of Growth/differentiation factor 11

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 11 between cysteines 371 and 404 (73 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 ?
35
PDB code
6mac
Structure name
ternary structure of gdf11 bound to actriib-ecd and alk5-ecd
Structure deposition date
2018-08-27
Thiol separation (Å)
10
Half-sphere exposure sum ?
62
Minimum pKa ?
9
% buried
nan
Peptide accession
O95390
Residue number A
371
Residue number B
404
Peptide name
Growth/differentiation factor 11

Ligandability

Cysteine 371 of Growth/differentiation factor 11

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 404 of Growth/differentiation factor 11

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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