ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

Growth/differentiation factor 5

Intermolecular
Cysteine 360 of Bone morphogenetic protein 2 and cysteine 465
Cysteine 465 and cysteine 465
Cysteine 329 of Bone morphogenetic protein 2 and cysteine 465
Cysteine 360 of Bone morphogenetic protein 2 and cysteine 466
Cysteine 360 of Bone morphogenetic protein 2 and cysteine 433
Cysteine 361 of Bone morphogenetic protein 2 and cysteine 465
Cysteine 360 of Bone morphogenetic protein 2 and cysteine 400
Cysteine 296 of Bone morphogenetic protein 2 and cysteine 465
Cysteine 360 of Bone morphogenetic protein 2 and cysteine 429
Cysteine 325 of Bone morphogenetic protein 2 and cysteine 465
More...
Cysteine 395 of Bone morphogenetic protein 2 and cysteine 465
Cysteine 360 of Bone morphogenetic protein 2 and cysteine 500
Intramolecular
Cysteine 400 and cysteine 466
Cysteine 433 and cysteine 500
Cysteine 429 and cysteine 498
Cysteine 400 and cysteine 433
Cysteine 400 and cysteine 500
Cysteine 429 and cysteine 466
Cysteine 433 and cysteine 466
Cysteine 400 and cysteine 498
Cysteine 466 and cysteine 498
Cysteine 400 and cysteine 429
Cysteine 466 and cysteine 500
Cysteine 433 and cysteine 465
Cysteine 465 and cysteine 466
Cysteine 400 and cysteine 465
Cysteine 498 and cysteine 500
Cysteine 429 and cysteine 433
Cysteine 429 and cysteine 465
Cysteine 433 and cysteine 498
Cysteine 465 and cysteine 500
Cysteine 429 and cysteine 500
A redox-regulated disulphide may form between cysteine 360 of Bone morphogenetic protein 2 and cysteine 465 of Growth/differentiation factor 5 (78 and 84 respectively in this structure).

Details

Redox score ?
75
PDB code
8e3g
Structure name
bmp2/gdf5 heterodimer
Structure deposition date
2022-08-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
84
Minimum pKa ?
nan
% buried
nan
Peptide A name
Bone morphogenetic protein 2
Peptide B name
Growth/differentiation factor 5
Peptide A accession
P12643
Peptide B accession
P43026
Peptide A residue number
360
Peptide B residue number
465

Ligandability

Cysteine 360 of Bone morphogenetic protein 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 465 of Growth/differentiation factor 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 5 at cysteines 465 and 465 (84 and 84 respectively in this structure).

Details

Redox score ?
75
PDB code
3qb4
Structure name
crystal structure of a tgf-beta ligand-receptor complex
Structure deposition date
2011-01-12
Thiol separation (Å)
2
Half-sphere exposure sum ?
83
Minimum pKa ?
nan
% buried
nan
Peptide A name
Growth/differentiation factor 5
Peptide B name
Growth/differentiation factor 5
Peptide A accession
P43026
Peptide B accession
P43026
Peptide A residue number
465
Peptide B residue number
465

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 cysteine 329 of Bone morphogenetic protein 2 and cysteine 465 of Growth/differentiation factor 5 (47 and 84 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
8e3g
Structure name
bmp2/gdf5 heterodimer
Structure deposition date
2022-08-17
Thiol separation (Å)
8
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide A name
Bone morphogenetic protein 2
Peptide B name
Growth/differentiation factor 5
Peptide A accession
P12643
Peptide B accession
P43026
Peptide A residue number
329
Peptide B residue number
465

Ligandability

Cysteine 329 of Bone morphogenetic protein 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 465 of Growth/differentiation factor 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 cysteine 360 of Bone morphogenetic protein 2 and cysteine 466 of Growth/differentiation factor 5 (78 and 85 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
8e3g
Structure name
bmp2/gdf5 heterodimer
Structure deposition date
2022-08-17
Thiol separation (Å)
8
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide A name
Bone morphogenetic protein 2
Peptide B name
Growth/differentiation factor 5
Peptide A accession
P12643
Peptide B accession
P43026
Peptide A residue number
360
Peptide B residue number
466

Ligandability

Cysteine 360 of Bone morphogenetic protein 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 466 of Growth/differentiation factor 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 cysteine 360 of Bone morphogenetic protein 2 and cysteine 433 of Growth/differentiation factor 5 (78 and 52 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
8e3g
Structure name
bmp2/gdf5 heterodimer
Structure deposition date
2022-08-17
Thiol separation (Å)
8
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide A name
Bone morphogenetic protein 2
Peptide B name
Growth/differentiation factor 5
Peptide A accession
P12643
Peptide B accession
P43026
Peptide A residue number
360
Peptide B residue number
433

Ligandability

Cysteine 360 of Bone morphogenetic protein 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 433 of Growth/differentiation factor 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 cysteine 361 of Bone morphogenetic protein 2 and cysteine 465 of Growth/differentiation factor 5 (79 and 84 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
8e3g
Structure name
bmp2/gdf5 heterodimer
Structure deposition date
2022-08-17
Thiol separation (Å)
8
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide A name
Bone morphogenetic protein 2
Peptide B name
Growth/differentiation factor 5
Peptide A accession
P12643
Peptide B accession
P43026
Peptide A residue number
361
Peptide B residue number
465

Ligandability

Cysteine 361 of Bone morphogenetic protein 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 465 of Growth/differentiation factor 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 cysteine 360 of Bone morphogenetic protein 2 and cysteine 400 of Growth/differentiation factor 5 (78 and 19 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
8e3g
Structure name
bmp2/gdf5 heterodimer
Structure deposition date
2022-08-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide A name
Bone morphogenetic protein 2
Peptide B name
Growth/differentiation factor 5
Peptide A accession
P12643
Peptide B accession
P43026
Peptide A residue number
360
Peptide B residue number
400

Ligandability

Cysteine 360 of Bone morphogenetic protein 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 400 of Growth/differentiation factor 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 cysteine 296 of Bone morphogenetic protein 2 and cysteine 465 of Growth/differentiation factor 5 (14 and 84 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
8e3g
Structure name
bmp2/gdf5 heterodimer
Structure deposition date
2022-08-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide A name
Bone morphogenetic protein 2
Peptide B name
Growth/differentiation factor 5
Peptide A accession
P12643
Peptide B accession
P43026
Peptide A residue number
296
Peptide B residue number
465

Ligandability

Cysteine 296 of Bone morphogenetic protein 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 465 of Growth/differentiation factor 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 cysteine 360 of Bone morphogenetic protein 2 and cysteine 429 of Growth/differentiation factor 5 (78 and 48 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
8e3g
Structure name
bmp2/gdf5 heterodimer
Structure deposition date
2022-08-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
83
Minimum pKa ?
nan
% buried
nan
Peptide A name
Bone morphogenetic protein 2
Peptide B name
Growth/differentiation factor 5
Peptide A accession
P12643
Peptide B accession
P43026
Peptide A residue number
360
Peptide B residue number
429

Ligandability

Cysteine 360 of Bone morphogenetic protein 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 429 of Growth/differentiation factor 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 cysteine 325 of Bone morphogenetic protein 2 and cysteine 465 of Growth/differentiation factor 5 (43 and 84 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
8e3g
Structure name
bmp2/gdf5 heterodimer
Structure deposition date
2022-08-17
Thiol separation (Å)
10
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide A name
Bone morphogenetic protein 2
Peptide B name
Growth/differentiation factor 5
Peptide A accession
P12643
Peptide B accession
P43026
Peptide A residue number
325
Peptide B residue number
465

Ligandability

Cysteine 325 of Bone morphogenetic protein 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 465 of Growth/differentiation factor 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 cysteine 395 of Bone morphogenetic protein 2 and cysteine 465 of Growth/differentiation factor 5 (113 and 84 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
8e3g
Structure name
bmp2/gdf5 heterodimer
Structure deposition date
2022-08-17
Thiol separation (Å)
10
Half-sphere exposure sum ?
83
Minimum pKa ?
nan
% buried
nan
Peptide A name
Bone morphogenetic protein 2
Peptide B name
Growth/differentiation factor 5
Peptide A accession
P12643
Peptide B accession
P43026
Peptide A residue number
395
Peptide B residue number
465

Ligandability

Cysteine 395 of Bone morphogenetic protein 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 465 of Growth/differentiation factor 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 cysteine 360 of Bone morphogenetic protein 2 and cysteine 500 of Growth/differentiation factor 5 (78 and 119 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
8e3g
Structure name
bmp2/gdf5 heterodimer
Structure deposition date
2022-08-17
Thiol separation (Å)
10
Half-sphere exposure sum ?
87
Minimum pKa ?
nan
% buried
nan
Peptide A name
Bone morphogenetic protein 2
Peptide B name
Growth/differentiation factor 5
Peptide A accession
P12643
Peptide B accession
P43026
Peptide A residue number
360
Peptide B residue number
500

Ligandability

Cysteine 360 of Bone morphogenetic protein 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 500 of Growth/differentiation factor 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 5 between cysteines 400 and 466 (19 and 85 respectively in this structure).

Details

Redox score ?
87
PDB code
3evs
Structure name
crystal structure of the gdf-5:bmp receptor ib complex
Structure deposition date
2008-10-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43026
Residue number A
400
Residue number B
466
Peptide name
Growth/differentiation factor 5

Ligandability

Cysteine 400 of Growth/differentiation factor 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 466 of Growth/differentiation factor 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 5 between cysteines 433 and 500 (52 and 119 respectively in this structure).

Details

Redox score ?
85
PDB code
3evs
Structure name
crystal structure of the gdf-5:bmp receptor ib complex
Structure deposition date
2008-10-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43026
Residue number A
433
Residue number B
500
Peptide name
Growth/differentiation factor 5

Ligandability

Cysteine 433 of Growth/differentiation factor 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 500 of Growth/differentiation factor 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 5 between cysteines 429 and 498 (48 and 117 respectively in this structure).

Details

Redox score ?
84
PDB code
3qb4
Structure name
crystal structure of a tgf-beta ligand-receptor complex
Structure deposition date
2011-01-12
Thiol separation (Å)
2
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43026
Residue number A
429
Residue number B
498
Peptide name
Growth/differentiation factor 5

Ligandability

Cysteine 429 of Growth/differentiation factor 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 498 of Growth/differentiation factor 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 5 between cysteines 400 and 433 (18 and 51 respectively in this structure).

Details

Redox score ?
74
PDB code
2bhk
Structure name
crystal structure of human growth and differentiation factor 5 (gdf5)
Structure deposition date
2005-01-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43026
Residue number A
400
Residue number B
433
Peptide name
Growth/differentiation factor 5

Ligandability

Cysteine 400 of Growth/differentiation factor 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 433 of Growth/differentiation factor 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 5 between cysteines 400 and 500 (19 and 119 respectively in this structure).

Details

Redox score ?
72
PDB code
8e3g
Structure name
bmp2/gdf5 heterodimer
Structure deposition date
2022-08-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43026
Residue number A
400
Residue number B
500
Peptide name
Growth/differentiation factor 5

Ligandability

Cysteine 400 of Growth/differentiation factor 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 500 of Growth/differentiation factor 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 5 between cysteines 429 and 466 (47 and 84 respectively in this structure).

Details

Redox score ?
71
PDB code
2bhk
Structure name
crystal structure of human growth and differentiation factor 5 (gdf5)
Structure deposition date
2005-01-12
Thiol separation (Å)
5
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43026
Residue number A
429
Residue number B
466
Peptide name
Growth/differentiation factor 5

Ligandability

Cysteine 429 of Growth/differentiation factor 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 466 of Growth/differentiation factor 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 5 between cysteines 433 and 466 (52 and 85 respectively in this structure).

Details

Redox score ?
70
PDB code
1waq
Structure name
crystal structure of human growth and differentiation factor 5 (gdf-5)
Structure deposition date
2004-10-27
Thiol separation (Å)
5
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43026
Residue number A
433
Residue number B
466
Peptide name
Growth/differentiation factor 5

Ligandability

Cysteine 433 of Growth/differentiation factor 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 466 of Growth/differentiation factor 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 5 between cysteines 400 and 498 (18 and 116 respectively in this structure).

Details

Redox score ?
67
PDB code
2bhk
Structure name
crystal structure of human growth and differentiation factor 5 (gdf5)
Structure deposition date
2005-01-12
Thiol separation (Å)
5
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43026
Residue number A
400
Residue number B
498
Peptide name
Growth/differentiation factor 5

Ligandability

Cysteine 400 of Growth/differentiation factor 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 498 of Growth/differentiation factor 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 5 between cysteines 466 and 498 (85 and 117 respectively in this structure).

Details

Redox score ?
66
PDB code
5hk5
Structure name
structure of the grem2-gdf5 inhibitory complex
Structure deposition date
2016-01-13
Thiol separation (Å)
5
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43026
Residue number A
466
Residue number B
498
Peptide name
Growth/differentiation factor 5

Ligandability

Cysteine 466 of Growth/differentiation factor 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 498 of Growth/differentiation factor 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 5 between cysteines 400 and 429 (19 and 48 respectively in this structure).

Details

Redox score ?
64
PDB code
8e3g
Structure name
bmp2/gdf5 heterodimer
Structure deposition date
2022-08-17
Thiol separation (Å)
6
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43026
Residue number A
400
Residue number B
429
Peptide name
Growth/differentiation factor 5

Ligandability

Cysteine 400 of Growth/differentiation factor 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 429 of Growth/differentiation factor 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 5 between cysteines 466 and 500 (85 and 119 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
8e3g
Structure name
bmp2/gdf5 heterodimer
Structure deposition date
2022-08-17
Thiol separation (Å)
6
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43026
Residue number A
466
Residue number B
500
Peptide name
Growth/differentiation factor 5

Ligandability

Cysteine 466 of Growth/differentiation factor 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 500 of Growth/differentiation factor 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 5 between cysteines 433 and 465 (52 and 84 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
3qb4
Structure name
crystal structure of a tgf-beta ligand-receptor complex
Structure deposition date
2011-01-12
Thiol separation (Å)
6
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43026
Residue number A
433
Residue number B
465
Peptide name
Growth/differentiation factor 5

Ligandability

Cysteine 433 of Growth/differentiation factor 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 465 of Growth/differentiation factor 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 5 between cysteines 465 and 466 (83 and 84 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
2bhk
Structure name
crystal structure of human growth and differentiation factor 5 (gdf5)
Structure deposition date
2005-01-12
Thiol separation (Å)
7
Half-sphere exposure sum ?
59
Minimum pKa ?
9
% buried
nan
Peptide accession
P43026
Residue number A
465
Residue number B
466
Peptide name
Growth/differentiation factor 5

Ligandability

Cysteine 465 of Growth/differentiation factor 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 466 of Growth/differentiation factor 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 5 between cysteines 400 and 465 (18 and 83 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
2bhk
Structure name
crystal structure of human growth and differentiation factor 5 (gdf5)
Structure deposition date
2005-01-12
Thiol separation (Å)
8
Half-sphere exposure sum ?
63
Minimum pKa ?
9
% buried
nan
Peptide accession
P43026
Residue number A
400
Residue number B
465
Peptide name
Growth/differentiation factor 5

Ligandability

Cysteine 400 of Growth/differentiation factor 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 465 of Growth/differentiation factor 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 5 between cysteines 498 and 500 (117 and 119 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
3evs
Structure name
crystal structure of the gdf-5:bmp receptor ib complex
Structure deposition date
2008-10-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43026
Residue number A
498
Residue number B
500
Peptide name
Growth/differentiation factor 5

Ligandability

Cysteine 498 of Growth/differentiation factor 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 500 of Growth/differentiation factor 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 5 between cysteines 429 and 433 (48 and 52 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
3qb4
Structure name
crystal structure of a tgf-beta ligand-receptor complex
Structure deposition date
2011-01-12
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43026
Residue number A
429
Residue number B
433
Peptide name
Growth/differentiation factor 5

Ligandability

Cysteine 429 of Growth/differentiation factor 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 433 of Growth/differentiation factor 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 5 between cysteines 429 and 465 (47 and 83 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
2bhk
Structure name
crystal structure of human growth and differentiation factor 5 (gdf5)
Structure deposition date
2005-01-12
Thiol separation (Å)
9
Half-sphere exposure sum ?
59
Minimum pKa ?
9
% buried
nan
Peptide accession
P43026
Residue number A
429
Residue number B
465
Peptide name
Growth/differentiation factor 5

Ligandability

Cysteine 429 of Growth/differentiation factor 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 465 of Growth/differentiation factor 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 5 between cysteines 433 and 498 (52 and 117 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
3qb4
Structure name
crystal structure of a tgf-beta ligand-receptor complex
Structure deposition date
2011-01-12
Thiol separation (Å)
9
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43026
Residue number A
433
Residue number B
498
Peptide name
Growth/differentiation factor 5

Ligandability

Cysteine 433 of Growth/differentiation factor 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 498 of Growth/differentiation factor 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 5 between cysteines 465 and 500 (84 and 119 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
8e3g
Structure name
bmp2/gdf5 heterodimer
Structure deposition date
2022-08-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
83
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43026
Residue number A
465
Residue number B
500
Peptide name
Growth/differentiation factor 5

Ligandability

Cysteine 465 of Growth/differentiation factor 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 500 of Growth/differentiation factor 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 5 between cysteines 429 and 500 (48 and 119 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
8e3g
Structure name
bmp2/gdf5 heterodimer
Structure deposition date
2022-08-17
Thiol separation (Å)
10
Half-sphere exposure sum ?
83
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43026
Residue number A
429
Residue number B
500
Peptide name
Growth/differentiation factor 5

Ligandability

Cysteine 429 of Growth/differentiation factor 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 500 of Growth/differentiation factor 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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: