ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Neurotrophin-4

Intermolecular
Cysteine 201 and cysteine 201
Cysteine 158 and cysteine 201
Intramolecular
Cysteine 97 and cysteine 170
Cysteine 141 and cysteine 199
Cysteine 158 and cysteine 170
Cysteine 97 and cysteine 158
Cysteine 97 and cysteine 199
Cysteine 170 and cysteine 199
Cysteine 97 and cysteine 201
Cysteine 170 and cysteine 201
More...
Cysteine 141 and cysteine 170
Cysteine 97 and cysteine 141
Cysteine 158 and cysteine 199
Cysteine 141 and cysteine 158
Cysteine 199 and cysteine 201
Cysteine 141 and cysteine 201
A redox-regulated disulphide may form between two units of Neurotrophin-4 at cysteines 201 and 201 (121 and 121 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
1b98
Structure name
neurotrophin 4 (homodimer)
Structure deposition date
1999-02-22
Thiol separation (Å)
7
Half-sphere exposure sum ?
98
Minimum pKa ?
nan
% buried
nan
Peptide A name
Neurotrophin-4
Peptide B name
Neurotrophin-4
Peptide A accession
P34130
Peptide B accession
P34130
Peptide A residue number
201
Peptide B residue number
201

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 Neurotrophin-4 at cysteines 158 and 201 (78 and 121 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
1b98
Structure name
neurotrophin 4 (homodimer)
Structure deposition date
1999-02-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
93
Minimum pKa ?
nan
% buried
nan
Peptide A name
Neurotrophin-4
Peptide B name
Neurotrophin-4
Peptide A accession
P34130
Peptide B accession
P34130
Peptide A residue number
158
Peptide B residue number
201

Ligandability

Cysteine 158 of Neurotrophin-4

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 201 of Neurotrophin-4

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Neurotrophin-4 between cysteines 97 and 170 (17 and 90 respectively in this structure).

Details

Redox score ?
85
PDB code
1b98
Structure name
neurotrophin 4 (homodimer)
Structure deposition date
1999-02-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
P34130
Residue number A
97
Residue number B
170
Peptide name
Neurotrophin-4

Ligandability

Cysteine 97 of Neurotrophin-4

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 170 of Neurotrophin-4

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Neurotrophin-4 between cysteines 141 and 199 (61 and 119 respectively in this structure).

Details

Redox score ?
83
PDB code
1b98
Structure name
neurotrophin 4 (homodimer)
Structure deposition date
1999-02-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
P34130
Residue number A
141
Residue number B
199
Peptide name
Neurotrophin-4

Ligandability

Cysteine 141 of Neurotrophin-4

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 199 of Neurotrophin-4

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Neurotrophin-4 between cysteines 158 and 170 (78 and 90 respectively in this structure).

Details

Redox score ?
76
PDB code
1b98
Structure name
neurotrophin 4 (homodimer)
Structure deposition date
1999-02-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
P34130
Residue number A
158
Residue number B
170
Peptide name
Neurotrophin-4

Ligandability

Cysteine 158 of Neurotrophin-4

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 170 of Neurotrophin-4

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Neurotrophin-4 between cysteines 97 and 158 (17 and 78 respectively in this structure).

Details

Redox score ?
76
PDB code
1b98
Structure name
neurotrophin 4 (homodimer)
Structure deposition date
1999-02-22
Thiol separation (Å)
3
Half-sphere exposure sum ?
83
Minimum pKa ?
nan
% buried
nan
Peptide accession
P34130
Residue number A
97
Residue number B
158
Peptide name
Neurotrophin-4

Ligandability

Cysteine 97 of Neurotrophin-4

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 158 of Neurotrophin-4

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Neurotrophin-4 between cysteines 97 and 199 (17 and 119 respectively in this structure).

Details

Redox score ?
69
PDB code
1b98
Structure name
neurotrophin 4 (homodimer)
Structure deposition date
1999-02-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
P34130
Residue number A
97
Residue number B
199
Peptide name
Neurotrophin-4

Ligandability

Cysteine 97 of Neurotrophin-4

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 199 of Neurotrophin-4

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Neurotrophin-4 between cysteines 170 and 199 (90 and 119 respectively in this structure).

Details

Redox score ?
65
PDB code
1hcf
Structure name
crystal structure of trkb-d5 bound to neurotrophin-4/5
Structure deposition date
2001-05-03
Thiol separation (Å)
5
Half-sphere exposure sum ?
84
Minimum pKa ?
nan
% buried
nan
Peptide accession
P34130
Residue number A
170
Residue number B
199
Peptide name
Neurotrophin-4

Ligandability

Cysteine 170 of Neurotrophin-4

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 199 of Neurotrophin-4

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Neurotrophin-4 between cysteines 97 and 201 (17 and 121 respectively in this structure).

Details

Redox score ?
65
PDB code
1hcf
Structure name
crystal structure of trkb-d5 bound to neurotrophin-4/5
Structure deposition date
2001-05-03
Thiol separation (Å)
5
Half-sphere exposure sum ?
94
Minimum pKa ?
nan
% buried
nan
Peptide accession
P34130
Residue number A
97
Residue number B
201
Peptide name
Neurotrophin-4

Ligandability

Cysteine 97 of Neurotrophin-4

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 201 of Neurotrophin-4

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Neurotrophin-4 between cysteines 170 and 201 (90 and 121 respectively in this structure).

Details

Redox score ?
63
PDB code
1hcf
Structure name
crystal structure of trkb-d5 bound to neurotrophin-4/5
Structure deposition date
2001-05-03
Thiol separation (Å)
5
Half-sphere exposure sum ?
91
Minimum pKa ?
nan
% buried
nan
Peptide accession
P34130
Residue number A
170
Residue number B
201
Peptide name
Neurotrophin-4

Ligandability

Cysteine 170 of Neurotrophin-4

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 201 of Neurotrophin-4

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Neurotrophin-4 between cysteines 141 and 170 (61 and 90 respectively in this structure).

Details

Redox score ?
63
PDB code
1b98
Structure name
neurotrophin 4 (homodimer)
Structure deposition date
1999-02-22
Thiol separation (Å)
6
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
P34130
Residue number A
141
Residue number B
170
Peptide name
Neurotrophin-4

Ligandability

Cysteine 141 of Neurotrophin-4

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 170 of Neurotrophin-4

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Neurotrophin-4 between cysteines 97 and 141 (17 and 61 respectively in this structure).

Details

Redox score ?
61
PDB code
1hcf
Structure name
crystal structure of trkb-d5 bound to neurotrophin-4/5
Structure deposition date
2001-05-03
Thiol separation (Å)
6
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
P34130
Residue number A
97
Residue number B
141
Peptide name
Neurotrophin-4

Ligandability

Cysteine 97 of Neurotrophin-4

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 141 of Neurotrophin-4

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Neurotrophin-4 between cysteines 158 and 199 (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 ?
48
PDB code
1hcf
Structure name
crystal structure of trkb-d5 bound to neurotrophin-4/5
Structure deposition date
2001-05-03
Thiol separation (Å)
8
Half-sphere exposure sum ?
88
Minimum pKa ?
nan
% buried
nan
Peptide accession
P34130
Residue number A
158
Residue number B
199
Peptide name
Neurotrophin-4

Ligandability

Cysteine 158 of Neurotrophin-4

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 199 of Neurotrophin-4

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Neurotrophin-4 between cysteines 141 and 158 (61 and 78 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
1b98
Structure name
neurotrophin 4 (homodimer)
Structure deposition date
1999-02-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
P34130
Residue number A
141
Residue number B
158
Peptide name
Neurotrophin-4

Ligandability

Cysteine 141 of Neurotrophin-4

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 158 of Neurotrophin-4

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Neurotrophin-4 between cysteines 199 and 201 (119 and 121 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
1hcf
Structure name
crystal structure of trkb-d5 bound to neurotrophin-4/5
Structure deposition date
2001-05-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
93
Minimum pKa ?
nan
% buried
nan
Peptide accession
P34130
Residue number A
199
Residue number B
201
Peptide name
Neurotrophin-4

Ligandability

Cysteine 199 of Neurotrophin-4

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 201 of Neurotrophin-4

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Neurotrophin-4 between cysteines 141 and 201 (61 and 121 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
1b98
Structure name
neurotrophin 4 (homodimer)
Structure deposition date
1999-02-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
P34130
Residue number A
141
Residue number B
201
Peptide name
Neurotrophin-4

Ligandability

Cysteine 141 of Neurotrophin-4

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 201 of Neurotrophin-4

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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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