ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Tryptophan 5-hydroxylase 2

Intramolecular
Cysteine 236 and cysteine 367
Cysteine 357 and cysteine 406
Cysteine 357 and cysteine 410
A redox-regulated disulphide may form within Tryptophan 5-hydroxylase 2 between cysteines 236 and 367.

Details

Redox score ?
66
PDB code
4v06
Structure name
crystal structure of human tryptophan hydroxylase 2 (tph2), catalytic domain
Structure deposition date
2014-09-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
76
Minimum pKa ?
9
% buried
88
Peptide accession
Q8IWU9
Residue number A
236
Residue number B
367
Peptide name
Tryptophan 5-hydroxylase 2

Ligandability

Cysteine 236 of Tryptophan 5-hydroxylase 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 367 of Tryptophan 5-hydroxylase 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Tryptophan 5-hydroxylase 2 between cysteines 357 and 406.

Details

Redox score ?
65
PDB code
4v06
Structure name
crystal structure of human tryptophan hydroxylase 2 (tph2), catalytic domain
Structure deposition date
2014-09-11
Thiol separation (Å)
5
Half-sphere exposure sum ?
71
Minimum pKa ?
10
% buried
47
Peptide accession
Q8IWU9
Residue number A
357
Residue number B
406
Peptide name
Tryptophan 5-hydroxylase 2

Ligandability

Cysteine 357 of Tryptophan 5-hydroxylase 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 406 of Tryptophan 5-hydroxylase 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Tryptophan 5-hydroxylase 2 between cysteines 357 and 410. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
4v06
Structure name
crystal structure of human tryptophan hydroxylase 2 (tph2), catalytic domain
Structure deposition date
2014-09-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
11
% buried
62
Peptide accession
Q8IWU9
Residue number A
357
Residue number B
410
Peptide name
Tryptophan 5-hydroxylase 2

Ligandability

Cysteine 357 of Tryptophan 5-hydroxylase 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 410 of Tryptophan 5-hydroxylase 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

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