ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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BDNF/NT-3 growth factors receptor

Intramolecular
Cysteine 302 and cysteine 345
Cysteine 557 and cysteine 561
Cysteine 557 and cysteine 607
Cysteine 331 and cysteine 345
A redox-regulated disulphide may form within BDNF/NT-3 growth factors receptor between cysteines 302 and 345.

Details

Redox score ?
79
PDB code
5mo9
Structure name
structure of human trkb receptor ligand binding domain in complex with the fab frgment of antibody ab20
Structure deposition date
2016-12-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16620
Residue number A
302
Residue number B
345
Peptide name
BDNF/NT-3 growth factors receptor

Ligandability

Cysteine 302 of BDNF/NT-3 growth factors receptor

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 345 of BDNF/NT-3 growth factors receptor

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 BDNF/NT-3 growth factors receptor between cysteines 557 and 561 (573 and 577 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
4at4
Structure name
crystal structure of trkb kinase domain in complex with ex429
Structure deposition date
2012-05-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
nan
Minimum pKa ?
9
% buried
20
Peptide accession
Q16620
Residue number A
557
Residue number B
561
Peptide name
BDNF/NT-3 growth factors receptor

Ligandability

Cysteine 557 of BDNF/NT-3 growth factors receptor

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 561 of BDNF/NT-3 growth factors receptor

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 BDNF/NT-3 growth factors receptor between cysteines 557 and 607 (573 and 623 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
4at5
Structure name
crystal structure of trkb kinase domain in complex with gw2580
Structure deposition date
2012-05-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
10
% buried
34
Peptide accession
Q16620
Residue number A
557
Residue number B
607
Peptide name
BDNF/NT-3 growth factors receptor

Ligandability

Cysteine 557 of BDNF/NT-3 growth factors receptor

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 607 of BDNF/NT-3 growth factors receptor

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 BDNF/NT-3 growth factors receptor between cysteines 331 and 345. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
1wwb
Structure name
ligand binding domain of human trkb receptor
Structure deposition date
1999-05-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
50
Minimum pKa ?
9
% buried
nan
Peptide accession
Q16620
Residue number A
331
Residue number B
345
Peptide name
BDNF/NT-3 growth factors receptor

Ligandability

Cysteine 331 of BDNF/NT-3 growth factors receptor

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 345 of BDNF/NT-3 growth factors receptor

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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