ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

Inhibin beta A chain

Intermolecular
Cysteine 390 and cysteine 390
Intramolecular
Cysteine 244 and cysteine 247
Cysteine 321 and cysteine 391
Cysteine 350 and cysteine 423
Cysteine 354 and cysteine 425
Cysteine 314 and cysteine 322
Cysteine 321 and cysteine 354
Cysteine 321 and cysteine 425
Cysteine 354 and cysteine 391
Cysteine 350 and cysteine 391
More...
Cysteine 391 and cysteine 423
Cysteine 354 and cysteine 390
Cysteine 391 and cysteine 425
Cysteine 321 and cysteine 350
Cysteine 321 and cysteine 423
Cysteine 314 and cysteine 423
Cysteine 321 and cysteine 322
Cysteine 314 and cysteine 391
Cysteine 322 and cysteine 391
Cysteine 314 and cysteine 350
Cysteine 314 and cysteine 321
Cysteine 350 and cysteine 354
Cysteine 322 and cysteine 350
Cysteine 423 and cysteine 425
Cysteine 354 and cysteine 423
Cysteine 321 and cysteine 390
Cysteine 350 and cysteine 425
Cysteine 390 and cysteine 391
Cysteine 390 and cysteine 425
Cysteine 350 and cysteine 390
Cysteine 322 and cysteine 354
Cysteine 322 and cysteine 425
Cysteine 322 and cysteine 423
A redox-regulated disulphide may form between two units of Inhibin beta A chain at cysteines 390 and 390 (80 and 80 respectively in this structure).

Details

Redox score ?
74
PDB code
2p6a
Structure name
the structure of the activin:follistatin 315 complex
Structure deposition date
2007-03-16
Thiol separation (Å)
3
Half-sphere exposure sum ?
70
Minimum pKa ?
7
% buried
69
Peptide A name
Inhibin beta A chain
Peptide B name
Inhibin beta A chain
Peptide A accession
P08476
Peptide B accession
P08476
Peptide A residue number
390
Peptide B residue number
390

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 within Inhibin beta A chain between cysteines 244 and 247.

Details

Redox score ?
88
PDB code
5hly
Structure name
structure of pro-activin a precursor at 2
Structure deposition date
2016-01-15
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08476
Residue number A
244
Residue number B
247
Peptide name
Inhibin beta A chain

Ligandability

Cysteine 244 of Inhibin beta A chain

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 247 of Inhibin beta A chain

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 Inhibin beta A chain between cysteines 321 and 391.

Details

Redox score ?
84
PDB code
7u5p
Structure name
crystal structure of the activin receptor type-2a ligand binding domain in complex with activin-a
Structure deposition date
2022-03-02
Thiol separation (Å)
2
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08476
Residue number A
321
Residue number B
391
Peptide name
Inhibin beta A chain

Ligandability

Cysteine 321 of Inhibin beta A chain

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 391 of Inhibin beta A chain

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 Inhibin beta A chain between cysteines 350 and 423.

Details

Redox score ?
83
PDB code
7u5p
Structure name
crystal structure of the activin receptor type-2a ligand binding domain in complex with activin-a
Structure deposition date
2022-03-02
Thiol separation (Å)
2
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08476
Residue number A
350
Residue number B
423
Peptide name
Inhibin beta A chain

Ligandability

Cysteine 350 of Inhibin beta A chain

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 423 of Inhibin beta A chain

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 Inhibin beta A chain between cysteines 354 and 425 (44 and 115 respectively in this structure).

Details

Redox score ?
82
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 ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08476
Residue number A
354
Residue number B
425
Peptide name
Inhibin beta A chain

Ligandability

Cysteine 354 of Inhibin beta A chain

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 425 of Inhibin beta A chain

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 Inhibin beta A chain between cysteines 314 and 322 (4 and 12 respectively in this structure).

Details

Redox score ?
79
PDB code
2p6a
Structure name
the structure of the activin:follistatin 315 complex
Structure deposition date
2007-03-16
Thiol separation (Å)
3
Half-sphere exposure sum ?
63
Minimum pKa ?
9
% buried
22
Peptide accession
P08476
Residue number A
314
Residue number B
322
Peptide name
Inhibin beta A chain

Ligandability

Cysteine 314 of Inhibin beta A chain

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 322 of Inhibin beta A chain

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 Inhibin beta A chain between cysteines 321 and 354 (11 and 44 respectively in this structure).

Details

Redox score ?
74
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 ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08476
Residue number A
321
Residue number B
354
Peptide name
Inhibin beta A chain

Ligandability

Cysteine 321 of Inhibin beta A chain

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 354 of Inhibin beta A chain

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 Inhibin beta A chain between cysteines 321 and 425.

Details

Redox score ?
72
PDB code
5hlz
Structure name
structure of pro-activin a complex at 2
Structure deposition date
2016-01-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08476
Residue number A
321
Residue number B
425
Peptide name
Inhibin beta A chain

Ligandability

Cysteine 321 of Inhibin beta A chain

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 425 of Inhibin beta A chain

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 Inhibin beta A chain between cysteines 354 and 391 (44 and 81 respectively in this structure).

Details

Redox score ?
71
PDB code
1nys
Structure name
crystal structure of activin a bound to the ecd of actriib p41
Structure deposition date
2003-02-13
Thiol separation (Å)
5
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08476
Residue number A
354
Residue number B
391
Peptide name
Inhibin beta A chain

Ligandability

Cysteine 354 of Inhibin beta A chain

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 391 of Inhibin beta A chain

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 Inhibin beta A chain between cysteines 350 and 391 (40 and 81 respectively in this structure).

Details

Redox score ?
70
PDB code
2p6a
Structure name
the structure of the activin:follistatin 315 complex
Structure deposition date
2007-03-16
Thiol separation (Å)
4
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08476
Residue number A
350
Residue number B
391
Peptide name
Inhibin beta A chain

Ligandability

Cysteine 350 of Inhibin beta A chain

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 391 of Inhibin beta A chain

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 Inhibin beta A chain between cysteines 391 and 423 (81 and 113 respectively in this structure).

Details

Redox score ?
69
PDB code
1nys
Structure name
crystal structure of activin a bound to the ecd of actriib p41
Structure deposition date
2003-02-13
Thiol separation (Å)
5
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08476
Residue number A
391
Residue number B
423
Peptide name
Inhibin beta A chain

Ligandability

Cysteine 391 of Inhibin beta A chain

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 423 of Inhibin beta A chain

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 Inhibin beta A chain between cysteines 354 and 390 (44 and 80 respectively in this structure).

Details

Redox score ?
68
PDB code
2arp
Structure name
activin a in complex with fs12 fragment of follistatin
Structure deposition date
2005-08-21
Thiol separation (Å)
6
Half-sphere exposure sum ?
39
Minimum pKa ?
9
% buried
nan
Peptide accession
P08476
Residue number A
354
Residue number B
390
Peptide name
Inhibin beta A chain

Ligandability

Cysteine 354 of Inhibin beta A chain

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 390 of Inhibin beta A chain

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 Inhibin beta A chain between cysteines 391 and 425 (81 and 115 respectively in this structure).

Details

Redox score ?
64
PDB code
1nys
Structure name
crystal structure of activin a bound to the ecd of actriib p41
Structure deposition date
2003-02-13
Thiol separation (Å)
5
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08476
Residue number A
391
Residue number B
425
Peptide name
Inhibin beta A chain

Ligandability

Cysteine 391 of Inhibin beta A chain

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 425 of Inhibin beta A chain

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 Inhibin beta A chain between cysteines 321 and 350 (11 and 40 respectively in this structure).

Details

Redox score ?
64
PDB code
1s4y
Structure name
crystal structure of the activin/actriib extracellular domain
Structure deposition date
2004-01-19
Thiol separation (Å)
6
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08476
Residue number A
321
Residue number B
350
Peptide name
Inhibin beta A chain

Ligandability

Cysteine 321 of Inhibin beta A chain

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 350 of Inhibin beta A chain

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 Inhibin beta A chain between cysteines 321 and 423 (11 and 113 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 ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08476
Residue number A
321
Residue number B
423
Peptide name
Inhibin beta A chain

Ligandability

Cysteine 321 of Inhibin beta A chain

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 423 of Inhibin beta A chain

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 Inhibin beta A chain between cysteines 314 and 423. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
5hlz
Structure name
structure of pro-activin a complex at 2
Structure deposition date
2016-01-15
Thiol separation (Å)
7
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08476
Residue number A
314
Residue number B
423
Peptide name
Inhibin beta A chain

Ligandability

Cysteine 314 of Inhibin beta A chain

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 423 of Inhibin beta A chain

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 Inhibin beta A chain between cysteines 321 and 322 (11 and 12 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 ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08476
Residue number A
321
Residue number B
322
Peptide name
Inhibin beta A chain

Ligandability

Cysteine 321 of Inhibin beta A chain

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 322 of Inhibin beta A chain

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 Inhibin beta A chain between cysteines 314 and 391 (4 and 81 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
2b0u
Structure name
the structure of the follistatin:activin complex
Structure deposition date
2005-09-14
Thiol separation (Å)
7
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08476
Residue number A
314
Residue number B
391
Peptide name
Inhibin beta A chain

Ligandability

Cysteine 314 of Inhibin beta A chain

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 391 of Inhibin beta A chain

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 Inhibin beta A chain between cysteines 322 and 391 (12 and 81 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
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 ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08476
Residue number A
322
Residue number B
391
Peptide name
Inhibin beta A chain

Ligandability

Cysteine 322 of Inhibin beta A chain

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 391 of Inhibin beta A chain

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 Inhibin beta A chain between cysteines 314 and 350. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
7u5p
Structure name
crystal structure of the activin receptor type-2a ligand binding domain in complex with activin-a
Structure deposition date
2022-03-02
Thiol separation (Å)
8
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08476
Residue number A
314
Residue number B
350
Peptide name
Inhibin beta A chain

Ligandability

Cysteine 314 of Inhibin beta A chain

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 350 of Inhibin beta A chain

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 Inhibin beta A chain between cysteines 314 and 321 (4 and 11 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
2p6a
Structure name
the structure of the activin:follistatin 315 complex
Structure deposition date
2007-03-16
Thiol separation (Å)
8
Half-sphere exposure sum ?
63
Minimum pKa ?
10
% buried
nan
Peptide accession
P08476
Residue number A
314
Residue number B
321
Peptide name
Inhibin beta A chain

Ligandability

Cysteine 314 of Inhibin beta A chain

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 321 of Inhibin beta A chain

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 Inhibin beta A chain between cysteines 350 and 354 (40 and 44 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
2p6a
Structure name
the structure of the activin:follistatin 315 complex
Structure deposition date
2007-03-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08476
Residue number A
350
Residue number B
354
Peptide name
Inhibin beta A chain

Ligandability

Cysteine 350 of Inhibin beta A chain

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 354 of Inhibin beta A chain

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 Inhibin beta A chain between cysteines 322 and 350. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
5hlz
Structure name
structure of pro-activin a complex at 2
Structure deposition date
2016-01-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08476
Residue number A
322
Residue number B
350
Peptide name
Inhibin beta A chain

Ligandability

Cysteine 322 of Inhibin beta A chain

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 350 of Inhibin beta A chain

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 Inhibin beta A chain between cysteines 423 and 425 (113 and 115 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
2arp
Structure name
activin a in complex with fs12 fragment of follistatin
Structure deposition date
2005-08-21
Thiol separation (Å)
10
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08476
Residue number A
423
Residue number B
425
Peptide name
Inhibin beta A chain

Ligandability

Cysteine 423 of Inhibin beta A chain

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 425 of Inhibin beta A chain

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 Inhibin beta A chain between cysteines 354 and 423 (44 and 113 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
2arv
Structure name
structure of human activin a
Structure deposition date
2005-08-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08476
Residue number A
354
Residue number B
423
Peptide name
Inhibin beta A chain

Ligandability

Cysteine 354 of Inhibin beta A chain

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 423 of Inhibin beta A chain

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 Inhibin beta A chain between cysteines 321 and 390 (11 and 80 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
2p6a
Structure name
the structure of the activin:follistatin 315 complex
Structure deposition date
2007-03-16
Thiol separation (Å)
10
Half-sphere exposure sum ?
76
Minimum pKa ?
7
% buried
nan
Peptide accession
P08476
Residue number A
321
Residue number B
390
Peptide name
Inhibin beta A chain

Ligandability

Cysteine 321 of Inhibin beta A chain

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 390 of Inhibin beta A chain

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 Inhibin beta A chain between cysteines 350 and 425. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
5hly
Structure name
structure of pro-activin a precursor at 2
Structure deposition date
2016-01-15
Thiol separation (Å)
10
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08476
Residue number A
350
Residue number B
425
Peptide name
Inhibin beta A chain

Ligandability

Cysteine 350 of Inhibin beta A chain

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 425 of Inhibin beta A chain

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 Inhibin beta A chain between cysteines 390 and 391 (80 and 81 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)
9
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08476
Residue number A
390
Residue number B
391
Peptide name
Inhibin beta A chain

Ligandability

Cysteine 390 of Inhibin beta A chain

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 391 of Inhibin beta A chain

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 Inhibin beta A chain between cysteines 390 and 425 (80 and 115 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
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 ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08476
Residue number A
390
Residue number B
425
Peptide name
Inhibin beta A chain

Ligandability

Cysteine 390 of Inhibin beta A chain

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 425 of Inhibin beta A chain

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 Inhibin beta A chain between cysteines 350 and 390 (40 and 80 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
2b0u
Structure name
the structure of the follistatin:activin complex
Structure deposition date
2005-09-14
Thiol separation (Å)
9
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08476
Residue number A
350
Residue number B
390
Peptide name
Inhibin beta A chain

Ligandability

Cysteine 350 of Inhibin beta A chain

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 390 of Inhibin beta A chain

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 Inhibin beta A chain between cysteines 322 and 354 (12 and 44 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
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 ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08476
Residue number A
322
Residue number B
354
Peptide name
Inhibin beta A chain

Ligandability

Cysteine 322 of Inhibin beta A chain

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 354 of Inhibin beta A chain

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 Inhibin beta A chain between cysteines 322 and 425 (12 and 115 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
2arp
Structure name
activin a in complex with fs12 fragment of follistatin
Structure deposition date
2005-08-21
Thiol separation (Å)
10
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08476
Residue number A
322
Residue number B
425
Peptide name
Inhibin beta A chain

Ligandability

Cysteine 322 of Inhibin beta A chain

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 425 of Inhibin beta A chain

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 Inhibin beta A chain between cysteines 322 and 423 (12 and 113 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
2p6a
Structure name
the structure of the activin:follistatin 315 complex
Structure deposition date
2007-03-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
74
Minimum pKa ?
12
% buried
nan
Peptide accession
P08476
Residue number A
322
Residue number B
423
Peptide name
Inhibin beta A chain

Ligandability

Cysteine 322 of Inhibin beta A chain

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 423 of Inhibin beta A chain

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.

If this tool was useful for finding a disulphide, please cite: