ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Prolyl 3-hydroxylase OGFOD1

Intramolecular
Cysteine 308 and cysteine 466
Cysteine 308 and cysteine 468
Cysteine 344 and cysteine 466
Cysteine 308 and cysteine 344
Cysteine 466 and cysteine 468
A redox-regulated disulphide may form within Prolyl 3-hydroxylase OGFOD1 between cysteines 308 and 466.

Details

Redox score ?
62
PDB code
4nhy
Structure name
crystal structure of human ogfod1, 2-oxoglutarate and iron-dependent oxygenase domain containing 1, in complex with pyridine-2,4- dicarboxylic acid (2,4-pdca)
Structure deposition date
2013-11-05
Thiol separation (Å)
5
Half-sphere exposure sum ?
77
Minimum pKa ?
9
% buried
98
Peptide accession
Q8N543
Residue number A
308
Residue number B
466
Peptide name
Prolyl 3-hydroxylase OGFOD1

Ligandability

Cysteine 308 of Prolyl 3-hydroxylase OGFOD1

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 466 of Prolyl 3-hydroxylase OGFOD1

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 Prolyl 3-hydroxylase OGFOD1 between cysteines 308 and 468. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
4nhx
Structure name
crystal structure of human ogfod1, 2-oxoglutarate and iron-dependent oxygenase domain containing 1, in complex with n-oxalylglycine (nog)
Structure deposition date
2013-11-05
Thiol separation (Å)
8
Half-sphere exposure sum ?
65
Minimum pKa ?
8
% buried
84
Peptide accession
Q8N543
Residue number A
308
Residue number B
468
Peptide name
Prolyl 3-hydroxylase OGFOD1

Ligandability

Cysteine 308 of Prolyl 3-hydroxylase OGFOD1

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 468 of Prolyl 3-hydroxylase OGFOD1

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 Prolyl 3-hydroxylase OGFOD1 between cysteines 344 and 466. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
4nhy
Structure name
crystal structure of human ogfod1, 2-oxoglutarate and iron-dependent oxygenase domain containing 1, in complex with pyridine-2,4- dicarboxylic acid (2,4-pdca)
Structure deposition date
2013-11-05
Thiol separation (Å)
7
Half-sphere exposure sum ?
74
Minimum pKa ?
13
% buried
100
Peptide accession
Q8N543
Residue number A
344
Residue number B
466
Peptide name
Prolyl 3-hydroxylase OGFOD1

Ligandability

Cysteine 344 of Prolyl 3-hydroxylase OGFOD1

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 466 of Prolyl 3-hydroxylase OGFOD1

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 Prolyl 3-hydroxylase OGFOD1 between cysteines 308 and 344. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
4nhx
Structure name
crystal structure of human ogfod1, 2-oxoglutarate and iron-dependent oxygenase domain containing 1, in complex with n-oxalylglycine (nog)
Structure deposition date
2013-11-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
70
Minimum pKa ?
8
% buried
87
Peptide accession
Q8N543
Residue number A
308
Residue number B
344
Peptide name
Prolyl 3-hydroxylase OGFOD1

Ligandability

Cysteine 308 of Prolyl 3-hydroxylase OGFOD1

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 344 of Prolyl 3-hydroxylase OGFOD1

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 Prolyl 3-hydroxylase OGFOD1 between cysteines 466 and 468. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
4nhy
Structure name
crystal structure of human ogfod1, 2-oxoglutarate and iron-dependent oxygenase domain containing 1, in complex with pyridine-2,4- dicarboxylic acid (2,4-pdca)
Structure deposition date
2013-11-05
Thiol separation (Å)
7
Half-sphere exposure sum ?
78
Minimum pKa ?
14
% buried
100
Peptide accession
Q8N543
Residue number A
466
Residue number B
468
Peptide name
Prolyl 3-hydroxylase OGFOD1

Ligandability

Cysteine 466 of Prolyl 3-hydroxylase OGFOD1

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 468 of Prolyl 3-hydroxylase OGFOD1

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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