ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Phenylalanine-4-hydroxylase

Intramolecular
Cysteine 203 and cysteine 334
Cysteine 334 and cysteine 357
Cysteine 203 and cysteine 357
Cysteine 217 and cysteine 237
A redox-regulated disulphide may form within Phenylalanine-4-hydroxylase between cysteines 203 and 334.

Details

Redox score ?
65
PDB code
6n1k
Structure name
full-length human phenylalanine hydroxylase (pah) in the resting state
Structure deposition date
2018-11-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
77
Minimum pKa ?
9
% buried
98
Peptide accession
P00439
Residue number A
203
Residue number B
334
Peptide name
Phenylalanine-4-hydroxylase

Ligandability

Cysteine 203 of Phenylalanine-4-hydroxylase

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 334 of Phenylalanine-4-hydroxylase

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 Phenylalanine-4-hydroxylase between cysteines 334 and 357. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
1tg2
Structure name
crystal structure of phenylalanine hydroxylase a313t mutant with 7,8- dihydrobiopterin bound
Structure deposition date
2004-05-28
Thiol separation (Å)
10
Half-sphere exposure sum ?
76
Minimum pKa ?
8
% buried
81
Peptide accession
P00439
Residue number A
334
Residue number B
357
Peptide name
Phenylalanine-4-hydroxylase

Ligandability

Cysteine 334 of Phenylalanine-4-hydroxylase

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 357 of Phenylalanine-4-hydroxylase

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 Phenylalanine-4-hydroxylase between cysteines 203 and 357. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
1tdw
Structure name
crystal structure of double truncated human phenylalanine hydroxylase bh4-responsive pku mutant a313t
Structure deposition date
2004-05-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
74
Minimum pKa ?
13
% buried
nan
Peptide accession
P00439
Residue number A
203
Residue number B
357
Peptide name
Phenylalanine-4-hydroxylase

Ligandability

Cysteine 203 of Phenylalanine-4-hydroxylase

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 357 of Phenylalanine-4-hydroxylase

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 Phenylalanine-4-hydroxylase between cysteines 217 and 237. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
6hyc
Structure name
the structure of full-length human phenylalanine hydroxylase in complex with the cofactor and negative regulator tetrahydrobiopterin
Structure deposition date
2018-10-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
72
Minimum pKa ?
12
% buried
94
Peptide accession
P00439
Residue number A
217
Residue number B
237
Peptide name
Phenylalanine-4-hydroxylase

Ligandability

Cysteine 217 of Phenylalanine-4-hydroxylase

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 237 of Phenylalanine-4-hydroxylase

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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