ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Trans-3-hydroxy-L-proline dehydratase

Intramolecular
Cysteine 104 and cysteine 137 L
Cysteine 104 and cysteine 139 L
Cysteine 137 and cysteine 139 L
A redox-regulated disulphide may form within Trans-3-hydroxy-L-proline dehydratase between cysteines 104 and 137.

Details

Redox score ?
83
PDB code
7qpo
Structure name
crystal structure of human trans-3-hydroxy-l-proline dehydratase
Structure deposition date
2022-01-05
Thiol separation (Å)
2
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96EM0
Residue number A
104
Residue number B
137
Peptide name
Trans-3-hydroxy-L-proline dehydratase

Ligandability

Cysteine 104 of Trans-3-hydroxy-L-proline dehydratase

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 137 of Trans-3-hydroxy-L-proline dehydratase

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Trans-3-hydroxy-L-proline dehydratase between cysteines 104 and 139.

Details

Redox score ?
66
PDB code
7qpo
Structure name
crystal structure of human trans-3-hydroxy-l-proline dehydratase
Structure deposition date
2022-01-05
Thiol separation (Å)
5
Half-sphere exposure sum ?
63
Minimum pKa ?
10
% buried
nan
Peptide accession
Q96EM0
Residue number A
104
Residue number B
139
Peptide name
Trans-3-hydroxy-L-proline dehydratase

Ligandability

Cysteine 104 of Trans-3-hydroxy-L-proline dehydratase

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 139 of Trans-3-hydroxy-L-proline dehydratase

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Trans-3-hydroxy-L-proline dehydratase between cysteines 137 and 139.

Details

Redox score ?
62
PDB code
7qpo
Structure name
crystal structure of human trans-3-hydroxy-l-proline dehydratase
Structure deposition date
2022-01-05
Thiol separation (Å)
5
Half-sphere exposure sum ?
67
Minimum pKa ?
10
% buried
nan
Peptide accession
Q96EM0
Residue number A
137
Residue number B
139
Peptide name
Trans-3-hydroxy-L-proline dehydratase

Ligandability

Cysteine 137 of Trans-3-hydroxy-L-proline dehydratase

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 139 of Trans-3-hydroxy-L-proline dehydratase

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.

Ligandable in the dataset of Kuljanin et al.

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