ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

Tryptophan 5-hydroxylase 1

Intramolecular
Cysteine 190 and cysteine 321
Cysteine 311 and cysteine 360
Cysteine 360 and cysteine 364
Cysteine 311 and cysteine 364
A redox-regulated disulphide may form within Tryptophan 5-hydroxylase 1 between cysteines 190 and 321.

Details

Redox score ?
75
PDB code
5j6d
Structure name
discovery of acyl guanidine tryptophan hydroxylase-1 inhibitors
Structure deposition date
2016-04-04
Thiol separation (Å)
4
Half-sphere exposure sum ?
nan
Minimum pKa ?
10
% buried
40
Peptide accession
P17752
Residue number A
190
Residue number B
321
Peptide name
Tryptophan 5-hydroxylase 1

Ligandability

Cysteine 190 of Tryptophan 5-hydroxylase 1

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 321 of Tryptophan 5-hydroxylase 1

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 1 between cysteines 311 and 360.

Details

Redox score ?
62
PDB code
3hfb
Structure name
crystal structure of human tryoptophan hydroxylase type 1 with lp- 534193
Structure deposition date
2009-05-11
Thiol separation (Å)
5
Half-sphere exposure sum ?
74
Minimum pKa ?
10
% buried
59
Peptide accession
P17752
Residue number A
311
Residue number B
360
Peptide name
Tryptophan 5-hydroxylase 1

Ligandability

Cysteine 311 of Tryptophan 5-hydroxylase 1

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 360 of Tryptophan 5-hydroxylase 1

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 1 between cysteines 360 and 364. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
1mlw
Structure name
crystal structure of human tryptophan hydroxylase with bound 7,8-dihydro-l-biopterin cofactor and fe(iii)
Structure deposition date
2002-08-31
Thiol separation (Å)
10
Half-sphere exposure sum ?
54
Minimum pKa ?
9
% buried
44
Peptide accession
P17752
Residue number A
360
Residue number B
364
Peptide name
Tryptophan 5-hydroxylase 1

Ligandability

Cysteine 360 of Tryptophan 5-hydroxylase 1

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 364 of Tryptophan 5-hydroxylase 1

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 1 between cysteines 311 and 364. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
3hf6
Structure name
crystal structure of human tryptophan hydroxylase type 1 with bound lp-521834 and fe
Structure deposition date
2009-05-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
11
% buried
79
Peptide accession
P17752
Residue number A
311
Residue number B
364
Peptide name
Tryptophan 5-hydroxylase 1

Ligandability

Cysteine 311 of Tryptophan 5-hydroxylase 1

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 364 of Tryptophan 5-hydroxylase 1

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: