ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Tyrosine 3-monooxygenase

Intramolecular
Cysteine 279 and cysteine 410
Cysteine 329 and cysteine 330
Cysteine 341 and cysteine 359
A redox-regulated disulphide may form within Tyrosine 3-monooxygenase between cysteines 279 and 410 (248 and 379 respectively in this structure).

Details

Redox score ?
76
PDB code
7pim
Structure name
partial structure of tyrosine hydroxylase lacking the first 35 residues in complex with dopamine
Structure deposition date
2021-08-20
Thiol separation (Å)
3
Half-sphere exposure sum ?
70
Minimum pKa ?
9
% buried
68
Peptide accession
P07101
Residue number A
279
Residue number B
410
Peptide name
Tyrosine 3-monooxygenase

Ligandability

Cysteine 279 of Tyrosine 3-monooxygenase

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 Tyrosine 3-monooxygenase

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 Tyrosine 3-monooxygenase between cysteines 329 and 330. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
59
PDB code
2toh
Structure name
tyrosine hydroxylase catalytic and tetramerization domains from rat
Structure deposition date
1998-08-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
87
Minimum pKa ?
11
% buried
100
Peptide accession
P04177
Residue number A
329
Residue number B
330
Peptide name
Tyrosine 3-monooxygenase

Ligandability

Cysteine 329 of Tyrosine 3-monooxygenase

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 330 of Tyrosine 3-monooxygenase

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 Tyrosine 3-monooxygenase between cysteines 341 and 359 (310 and 328 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
7a2g
Structure name
full-length structure of the substrate-free tyrosine hydroxylase (apo- th)
Structure deposition date
2020-08-17
Thiol separation (Å)
8
Half-sphere exposure sum ?
73
Minimum pKa ?
14
% buried
100
Peptide accession
P07101
Residue number A
341
Residue number B
359
Peptide name
Tyrosine 3-monooxygenase

Ligandability

Cysteine 341 of Tyrosine 3-monooxygenase

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 359 of Tyrosine 3-monooxygenase

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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