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a tool for identifying drug-targetable redox-active disulphides

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Growth/differentiation factor 2

Intermolecular
Cysteine 392 and cysteine 392
Cysteine 356 and cysteine 392
Intramolecular
Cysteine 156 and cysteine 237
Cysteine 327 and cysteine 393
Cysteine 360 and cysteine 428
Cysteine 356 and cysteine 426
Cysteine 327 and cysteine 360
Cysteine 327 and cysteine 428
Cysteine 393 and cysteine 426
Cysteine 360 and cysteine 393
More...
Cysteine 356 and cysteine 393
Cysteine 393 and cysteine 428
Cysteine 327 and cysteine 426
Cysteine 327 and cysteine 356
Cysteine 360 and cysteine 392
Cysteine 356 and cysteine 428
Cysteine 327 and cysteine 392
Cysteine 356 and cysteine 360
Cysteine 360 and cysteine 426
Cysteine 426 and cysteine 428
Cysteine 392 and cysteine 428
Cysteine 392 and cysteine 393
A redox-regulated disulphide may form between two units of Growth/differentiation factor 2 at cysteines 392 and 392 (370 and 370 respectively in this structure).

Details

Redox score ?
60
PDB code
4ycg
Structure name
pro-bone morphogenetic protein 9
Structure deposition date
2015-02-20
Thiol separation (Å)
5
Half-sphere exposure sum ?
84
Minimum pKa ?
8
% buried
90
Peptide A name
Growth/differentiation factor 2
Peptide B name
Growth/differentiation factor 2
Peptide A accession
Q9UK05
Peptide B accession
Q9UK05
Peptide A residue number
392
Peptide B residue number
392

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 2 at cysteines 356 and 392 (334 and 370 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
4yci
Structure name
non-latent pro-bone morphogenetic protein 9
Structure deposition date
2015-02-20
Thiol separation (Å)
9
Half-sphere exposure sum ?
79
Minimum pKa ?
8
% buried
nan
Peptide A name
Growth/differentiation factor 2
Peptide B name
Growth/differentiation factor 2
Peptide A accession
Q9UK05
Peptide B accession
Q9UK05
Peptide A residue number
356
Peptide B residue number
392

Ligandability

Cysteine 356 of Growth/differentiation factor 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 392 of Growth/differentiation factor 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 2 between cysteines 156 and 237.

Details

Redox score ?
88
PDB code
6sf2
Structure name
ternary complex of human bone morphogenetic protein 9 (bmp9) growth factor domain, its prodomain and extracellular domain of activin receptor-like kinase 1 (alk1)
Structure deposition date
2019-07-31
Thiol separation (Å)
2
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UK05
Residue number A
156
Residue number B
237
Peptide name
Growth/differentiation factor 2

Ligandability

Cysteine 156 of Growth/differentiation factor 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 237 of Growth/differentiation factor 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 2 between cysteines 327 and 393.

Details

Redox score ?
84
PDB code
6sf2
Structure name
ternary complex of human bone morphogenetic protein 9 (bmp9) growth factor domain, its prodomain and extracellular domain of activin receptor-like kinase 1 (alk1)
Structure deposition date
2019-07-31
Thiol separation (Å)
2
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UK05
Residue number A
327
Residue number B
393
Peptide name
Growth/differentiation factor 2

Ligandability

Cysteine 327 of Growth/differentiation factor 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 393 of Growth/differentiation factor 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 2 between cysteines 360 and 428 (41 and 109 respectively in this structure).

Details

Redox score ?
84
PDB code
4fao
Structure name
specificity and structure of a high affinity activin-like 1 (alk1) signaling complex
Structure deposition date
2012-05-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UK05
Residue number A
360
Residue number B
428
Peptide name
Growth/differentiation factor 2

Ligandability

Cysteine 360 of Growth/differentiation factor 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 428 of Growth/differentiation factor 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 2 between cysteines 356 and 426 (37 and 107 respectively in this structure).

Details

Redox score ?
83
PDB code
4fao
Structure name
specificity and structure of a high affinity activin-like 1 (alk1) signaling complex
Structure deposition date
2012-05-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UK05
Residue number A
356
Residue number B
426
Peptide name
Growth/differentiation factor 2

Ligandability

Cysteine 356 of Growth/differentiation factor 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 426 of Growth/differentiation factor 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 2 between cysteines 327 and 360 (8 and 41 respectively in this structure).

Details

Redox score ?
72
PDB code
4fao
Structure name
specificity and structure of a high affinity activin-like 1 (alk1) signaling complex
Structure deposition date
2012-05-22
Thiol separation (Å)
5
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UK05
Residue number A
327
Residue number B
360
Peptide name
Growth/differentiation factor 2

Ligandability

Cysteine 327 of Growth/differentiation factor 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 360 of Growth/differentiation factor 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 2 between cysteines 327 and 428 (8 and 109 respectively in this structure).

Details

Redox score ?
70
PDB code
4fao
Structure name
specificity and structure of a high affinity activin-like 1 (alk1) signaling complex
Structure deposition date
2012-05-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UK05
Residue number A
327
Residue number B
428
Peptide name
Growth/differentiation factor 2

Ligandability

Cysteine 327 of Growth/differentiation factor 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 428 of Growth/differentiation factor 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 2 between cysteines 393 and 426 (74 and 107 respectively in this structure).

Details

Redox score ?
66
PDB code
4fao
Structure name
specificity and structure of a high affinity activin-like 1 (alk1) signaling complex
Structure deposition date
2012-05-22
Thiol separation (Å)
5
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UK05
Residue number A
393
Residue number B
426
Peptide name
Growth/differentiation factor 2

Ligandability

Cysteine 393 of Growth/differentiation factor 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 426 of Growth/differentiation factor 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 2 between cysteines 360 and 393 (41 and 74 respectively in this structure).

Details

Redox score ?
66
PDB code
4fao
Structure name
specificity and structure of a high affinity activin-like 1 (alk1) signaling complex
Structure deposition date
2012-05-22
Thiol separation (Å)
5
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UK05
Residue number A
360
Residue number B
393
Peptide name
Growth/differentiation factor 2

Ligandability

Cysteine 360 of Growth/differentiation factor 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 393 of Growth/differentiation factor 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 2 between cysteines 356 and 393 (37 and 74 respectively in this structure).

Details

Redox score ?
65
PDB code
4fao
Structure name
specificity and structure of a high affinity activin-like 1 (alk1) signaling complex
Structure deposition date
2012-05-22
Thiol separation (Å)
5
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UK05
Residue number A
356
Residue number B
393
Peptide name
Growth/differentiation factor 2

Ligandability

Cysteine 356 of Growth/differentiation factor 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 393 of Growth/differentiation factor 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 2 between cysteines 393 and 428 (74 and 109 respectively in this structure).

Details

Redox score ?
65
PDB code
5hzw
Structure name
crystal structure of the orphan region of human endoglin/cd105 in complex with bmp9
Structure deposition date
2016-02-03
Thiol separation (Å)
5
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UK05
Residue number A
393
Residue number B
428
Peptide name
Growth/differentiation factor 2

Ligandability

Cysteine 393 of Growth/differentiation factor 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 428 of Growth/differentiation factor 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 2 between cysteines 327 and 426 (8 and 107 respectively in this structure).

Details

Redox score ?
65
PDB code
4fao
Structure name
specificity and structure of a high affinity activin-like 1 (alk1) signaling complex
Structure deposition date
2012-05-22
Thiol separation (Å)
6
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UK05
Residue number A
327
Residue number B
426
Peptide name
Growth/differentiation factor 2

Ligandability

Cysteine 327 of Growth/differentiation factor 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 426 of Growth/differentiation factor 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 2 between cysteines 327 and 356.

Details

Redox score ?
64
PDB code
6sf2
Structure name
ternary complex of human bone morphogenetic protein 9 (bmp9) growth factor domain, its prodomain and extracellular domain of activin receptor-like kinase 1 (alk1)
Structure deposition date
2019-07-31
Thiol separation (Å)
6
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UK05
Residue number A
327
Residue number B
356
Peptide name
Growth/differentiation factor 2

Ligandability

Cysteine 327 of Growth/differentiation factor 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 356 of Growth/differentiation factor 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 2 between cysteines 360 and 392 (41 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 ?
52
PDB code
4mpl
Structure name
crystal structure of bmp9 at 1
Structure deposition date
2013-09-13
Thiol separation (Å)
7
Half-sphere exposure sum ?
66
Minimum pKa ?
9
% buried
nan
Peptide accession
Q9UK05
Residue number A
360
Residue number B
392
Peptide name
Growth/differentiation factor 2

Ligandability

Cysteine 360 of Growth/differentiation factor 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 392 of Growth/differentiation factor 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 2 between cysteines 356 and 428 (37 and 109 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
5hzw
Structure name
crystal structure of the orphan region of human endoglin/cd105 in complex with bmp9
Structure deposition date
2016-02-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UK05
Residue number A
356
Residue number B
428
Peptide name
Growth/differentiation factor 2

Ligandability

Cysteine 356 of Growth/differentiation factor 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 428 of Growth/differentiation factor 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 2 between cysteines 327 and 392 (8 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 ?
43
PDB code
4fao
Structure name
specificity and structure of a high affinity activin-like 1 (alk1) signaling complex
Structure deposition date
2012-05-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UK05
Residue number A
327
Residue number B
392
Peptide name
Growth/differentiation factor 2

Ligandability

Cysteine 327 of Growth/differentiation factor 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 392 of Growth/differentiation factor 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 2 between cysteines 356 and 360 (37 and 41 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
5i05
Structure name
crystal structure of human bmp9 at 1
Structure deposition date
2016-02-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UK05
Residue number A
356
Residue number B
360
Peptide name
Growth/differentiation factor 2

Ligandability

Cysteine 356 of Growth/differentiation factor 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 360 of Growth/differentiation factor 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 2 between cysteines 360 and 426. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
6sf2
Structure name
ternary complex of human bone morphogenetic protein 9 (bmp9) growth factor domain, its prodomain and extracellular domain of activin receptor-like kinase 1 (alk1)
Structure deposition date
2019-07-31
Thiol separation (Å)
10
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UK05
Residue number A
360
Residue number B
426
Peptide name
Growth/differentiation factor 2

Ligandability

Cysteine 360 of Growth/differentiation factor 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 426 of Growth/differentiation factor 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 2 between cysteines 426 and 428 (107 and 109 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
4fao
Structure name
specificity and structure of a high affinity activin-like 1 (alk1) signaling complex
Structure deposition date
2012-05-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UK05
Residue number A
426
Residue number B
428
Peptide name
Growth/differentiation factor 2

Ligandability

Cysteine 426 of Growth/differentiation factor 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 428 of Growth/differentiation factor 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 2 between cysteines 392 and 428. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
6sf2
Structure name
ternary complex of human bone morphogenetic protein 9 (bmp9) growth factor domain, its prodomain and extracellular domain of activin receptor-like kinase 1 (alk1)
Structure deposition date
2019-07-31
Thiol separation (Å)
8
Half-sphere exposure sum ?
86
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UK05
Residue number A
392
Residue number B
428
Peptide name
Growth/differentiation factor 2

Ligandability

Cysteine 392 of Growth/differentiation factor 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 428 of Growth/differentiation factor 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 2 between cysteines 392 and 393. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
6sf2
Structure name
ternary complex of human bone morphogenetic protein 9 (bmp9) growth factor domain, its prodomain and extracellular domain of activin receptor-like kinase 1 (alk1)
Structure deposition date
2019-07-31
Thiol separation (Å)
9
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UK05
Residue number A
392
Residue number B
393
Peptide name
Growth/differentiation factor 2

Ligandability

Cysteine 392 of Growth/differentiation factor 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 393 of Growth/differentiation factor 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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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