ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Neurotrophin-3

Intermolecular
Cysteine 248 and cysteine 248
Cysteine 239 of Brain-derived neurotrophic factor and cysteine 248
Cysteine 239 of Brain-derived neurotrophic factor and cysteine 152
Cysteine 205 and cysteine 248
Cysteine 141 of Brain-derived neurotrophic factor and cysteine 248
Cysteine 196 of Brain-derived neurotrophic factor and cysteine 248
Cysteine 239 of Brain-derived neurotrophic factor and cysteine 205
Intramolecular
Cysteine 195 and cysteine 246
Cysteine 152 and cysteine 217
Cysteine 205 and cysteine 217
More...
Cysteine 152 and cysteine 205
Cysteine 152 and cysteine 248
Cysteine 152 and cysteine 246
Cysteine 195 and cysteine 217
Cysteine 217 and cysteine 248
Cysteine 217 and cysteine 246
Cysteine 152 and cysteine 195
Cysteine 205 and cysteine 246
Cysteine 195 and cysteine 205
Cysteine 246 and cysteine 248
Cysteine 195 and cysteine 248
A redox-regulated disulphide may form between two units of Neurotrophin-3 at cysteines 248 and 248 (110 and 110 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
3buk
Structure name
crystal structure of the neurotrophin-3 and p75ntr symmetrical complex
Structure deposition date
2008-01-02
Thiol separation (Å)
8
Half-sphere exposure sum ?
90
Minimum pKa ?
nan
% buried
nan
Peptide A name
Neurotrophin-3
Peptide B name
Neurotrophin-3
Peptide A accession
P20783
Peptide B accession
P20783
Peptide A residue number
248
Peptide B residue number
248

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 239 of Brain-derived neurotrophic factor and cysteine 248 of Neurotrophin-3 (111 and 110 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
1bnd
Structure name
structure of the brain-derived neurotrophic factor(slash)neurotrophin 3 heterodimer
Structure deposition date
1994-12-12
Thiol separation (Å)
8
Half-sphere exposure sum ?
90
Minimum pKa ?
nan
% buried
nan
Peptide A name
Brain-derived neurotrophic factor
Peptide B name
Neurotrophin-3
Peptide A accession
P23560
Peptide B accession
P20783
Peptide A residue number
239
Peptide B residue number
248

Ligandability

Cysteine 239 of Brain-derived neurotrophic factor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 248 of Neurotrophin-3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 239 of Brain-derived neurotrophic factor and cysteine 152 of Neurotrophin-3 (111 and 14 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
1bnd
Structure name
structure of the brain-derived neurotrophic factor(slash)neurotrophin 3 heterodimer
Structure deposition date
1994-12-12
Thiol separation (Å)
9
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide A name
Brain-derived neurotrophic factor
Peptide B name
Neurotrophin-3
Peptide A accession
P23560
Peptide B accession
P20783
Peptide A residue number
239
Peptide B residue number
152

Ligandability

Cysteine 239 of Brain-derived neurotrophic factor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 152 of Neurotrophin-3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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-3 at cysteines 205 and 248 (67 and 110 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
3buk
Structure name
crystal structure of the neurotrophin-3 and p75ntr symmetrical complex
Structure deposition date
2008-01-02
Thiol separation (Å)
9
Half-sphere exposure sum ?
89
Minimum pKa ?
nan
% buried
nan
Peptide A name
Neurotrophin-3
Peptide B name
Neurotrophin-3
Peptide A accession
P20783
Peptide B accession
P20783
Peptide A residue number
205
Peptide B residue number
248

Ligandability

Cysteine 205 of Neurotrophin-3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 248 of Neurotrophin-3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 141 of Brain-derived neurotrophic factor and cysteine 248 of Neurotrophin-3 (13 and 110 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
1bnd
Structure name
structure of the brain-derived neurotrophic factor(slash)neurotrophin 3 heterodimer
Structure deposition date
1994-12-12
Thiol separation (Å)
9
Half-sphere exposure sum ?
84
Minimum pKa ?
nan
% buried
nan
Peptide A name
Brain-derived neurotrophic factor
Peptide B name
Neurotrophin-3
Peptide A accession
P23560
Peptide B accession
P20783
Peptide A residue number
141
Peptide B residue number
248

Ligandability

Cysteine 141 of Brain-derived neurotrophic factor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 248 of Neurotrophin-3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 196 of Brain-derived neurotrophic factor and cysteine 248 of Neurotrophin-3 (68 and 110 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
1bnd
Structure name
structure of the brain-derived neurotrophic factor(slash)neurotrophin 3 heterodimer
Structure deposition date
1994-12-12
Thiol separation (Å)
9
Half-sphere exposure sum ?
87
Minimum pKa ?
nan
% buried
nan
Peptide A name
Brain-derived neurotrophic factor
Peptide B name
Neurotrophin-3
Peptide A accession
P23560
Peptide B accession
P20783
Peptide A residue number
196
Peptide B residue number
248

Ligandability

Cysteine 196 of Brain-derived neurotrophic factor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 248 of Neurotrophin-3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 239 of Brain-derived neurotrophic factor and cysteine 205 of Neurotrophin-3 (111 and 67 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
1bnd
Structure name
structure of the brain-derived neurotrophic factor(slash)neurotrophin 3 heterodimer
Structure deposition date
1994-12-12
Thiol separation (Å)
9
Half-sphere exposure sum ?
85
Minimum pKa ?
nan
% buried
nan
Peptide A name
Brain-derived neurotrophic factor
Peptide B name
Neurotrophin-3
Peptide A accession
P23560
Peptide B accession
P20783
Peptide A residue number
239
Peptide B residue number
205

Ligandability

Cysteine 239 of Brain-derived neurotrophic factor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 205 of Neurotrophin-3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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-3 between cysteines 195 and 246 (57 and 108 respectively in this structure).

Details

Redox score ?
87
PDB code
1nt3
Structure name
human neurotrophin-3
Structure deposition date
1999-05-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P20783
Residue number A
195
Residue number B
246
Peptide name
Neurotrophin-3

Ligandability

Cysteine 195 of Neurotrophin-3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 246 of Neurotrophin-3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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-3 between cysteines 152 and 217 (14 and 79 respectively in this structure).

Details

Redox score ?
85
PDB code
3buk
Structure name
crystal structure of the neurotrophin-3 and p75ntr symmetrical complex
Structure deposition date
2008-01-02
Thiol separation (Å)
2
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P20783
Residue number A
152
Residue number B
217
Peptide name
Neurotrophin-3

Ligandability

Cysteine 152 of Neurotrophin-3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 217 of Neurotrophin-3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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-3 between cysteines 205 and 217 (67 and 79 respectively in this structure).

Details

Redox score ?
75
PDB code
1bnd
Structure name
structure of the brain-derived neurotrophic factor(slash)neurotrophin 3 heterodimer
Structure deposition date
1994-12-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
P20783
Residue number A
205
Residue number B
217
Peptide name
Neurotrophin-3

Ligandability

Cysteine 205 of Neurotrophin-3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 217 of Neurotrophin-3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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-3 between cysteines 152 and 205 (14 and 67 respectively in this structure).

Details

Redox score ?
75
PDB code
3buk
Structure name
crystal structure of the neurotrophin-3 and p75ntr symmetrical complex
Structure deposition date
2008-01-02
Thiol separation (Å)
4
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide accession
P20783
Residue number A
152
Residue number B
205
Peptide name
Neurotrophin-3

Ligandability

Cysteine 152 of Neurotrophin-3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 205 of Neurotrophin-3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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-3 between cysteines 152 and 248 (14 and 110 respectively in this structure).

Details

Redox score ?
72
PDB code
1nt3
Structure name
human neurotrophin-3
Structure deposition date
1999-05-17
Thiol separation (Å)
5
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P20783
Residue number A
152
Residue number B
248
Peptide name
Neurotrophin-3

Ligandability

Cysteine 152 of Neurotrophin-3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 248 of Neurotrophin-3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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-3 between cysteines 152 and 246 (14 and 108 respectively in this structure).

Details

Redox score ?
68
PDB code
3buk
Structure name
crystal structure of the neurotrophin-3 and p75ntr symmetrical complex
Structure deposition date
2008-01-02
Thiol separation (Å)
4
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
P20783
Residue number A
152
Residue number B
246
Peptide name
Neurotrophin-3

Ligandability

Cysteine 152 of Neurotrophin-3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 246 of Neurotrophin-3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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-3 between cysteines 195 and 217 (57 and 79 respectively in this structure).

Details

Redox score ?
68
PDB code
1b8k
Structure name
neurotrophin-3 from human
Structure deposition date
1999-02-01
Thiol separation (Å)
5
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
P20783
Residue number A
195
Residue number B
217
Peptide name
Neurotrophin-3

Ligandability

Cysteine 195 of Neurotrophin-3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 217 of Neurotrophin-3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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-3 between cysteines 217 and 248 (79 and 110 respectively in this structure).

Details

Redox score ?
67
PDB code
1b8k
Structure name
neurotrophin-3 from human
Structure deposition date
1999-02-01
Thiol separation (Å)
6
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
P20783
Residue number A
217
Residue number B
248
Peptide name
Neurotrophin-3

Ligandability

Cysteine 217 of Neurotrophin-3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 248 of Neurotrophin-3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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-3 between cysteines 217 and 246 (79 and 108 respectively in this structure).

Details

Redox score ?
67
PDB code
1bnd
Structure name
structure of the brain-derived neurotrophic factor(slash)neurotrophin 3 heterodimer
Structure deposition date
1994-12-12
Thiol separation (Å)
5
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
P20783
Residue number A
217
Residue number B
246
Peptide name
Neurotrophin-3

Ligandability

Cysteine 217 of Neurotrophin-3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 246 of Neurotrophin-3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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-3 between cysteines 152 and 195 (14 and 57 respectively in this structure).

Details

Redox score ?
65
PDB code
1bnd
Structure name
structure of the brain-derived neurotrophic factor(slash)neurotrophin 3 heterodimer
Structure deposition date
1994-12-12
Thiol separation (Å)
6
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P20783
Residue number A
152
Residue number B
195
Peptide name
Neurotrophin-3

Ligandability

Cysteine 152 of Neurotrophin-3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 195 of Neurotrophin-3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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-3 between cysteines 205 and 246 (67 and 108 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
1b8k
Structure name
neurotrophin-3 from human
Structure deposition date
1999-02-01
Thiol separation (Å)
8
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
P20783
Residue number A
205
Residue number B
246
Peptide name
Neurotrophin-3

Ligandability

Cysteine 205 of Neurotrophin-3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 246 of Neurotrophin-3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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-3 between cysteines 195 and 205 (57 and 67 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
1nt3
Structure name
human neurotrophin-3
Structure deposition date
1999-05-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P20783
Residue number A
195
Residue number B
205
Peptide name
Neurotrophin-3

Ligandability

Cysteine 195 of Neurotrophin-3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 205 of Neurotrophin-3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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-3 between cysteines 246 and 248 (108 and 110 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
3buk
Structure name
crystal structure of the neurotrophin-3 and p75ntr symmetrical complex
Structure deposition date
2008-01-02
Thiol separation (Å)
8
Half-sphere exposure sum ?
85
Minimum pKa ?
nan
% buried
nan
Peptide accession
P20783
Residue number A
246
Residue number B
248
Peptide name
Neurotrophin-3

Ligandability

Cysteine 246 of Neurotrophin-3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 248 of Neurotrophin-3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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-3 between cysteines 195 and 248 (57 and 110 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
1b8k
Structure name
neurotrophin-3 from human
Structure deposition date
1999-02-01
Thiol separation (Å)
10
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
P20783
Residue number A
195
Residue number B
248
Peptide name
Neurotrophin-3

Ligandability

Cysteine 195 of Neurotrophin-3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 248 of Neurotrophin-3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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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