ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Prolyl hydroxylase EGLN2

Intramolecular
Cysteine 185 and cysteine 192
Cysteine 192 and cysteine 267
Cysteine 267 and cysteine 310
Cysteine 192 and cysteine 310
Cysteine 307 and cysteine 310
A redox-regulated disulphide may form within Prolyl hydroxylase EGLN2 between cysteines 185 and 192.

Details

Redox score ?
70
PDB code
5v1b
Structure name
structure of phd1 in complex with 1,2,4-triazolo-[1,5-a]pyridine
Structure deposition date
2017-03-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
10
% buried
55
Peptide accession
Q96KS0
Residue number A
185
Residue number B
192
Peptide name
Prolyl hydroxylase EGLN2

Ligandability

Cysteine 185 of Prolyl hydroxylase EGLN2

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 192 of Prolyl hydroxylase EGLN2

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 hydroxylase EGLN2 between cysteines 192 and 267. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
5v1b
Structure name
structure of phd1 in complex with 1,2,4-triazolo-[1,5-a]pyridine
Structure deposition date
2017-03-01
Thiol separation (Å)
8
Half-sphere exposure sum ?
64
Minimum pKa ?
12
% buried
76
Peptide accession
Q96KS0
Residue number A
192
Residue number B
267
Peptide name
Prolyl hydroxylase EGLN2

Ligandability

Cysteine 192 of Prolyl hydroxylase EGLN2

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 267 of Prolyl hydroxylase EGLN2

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 hydroxylase EGLN2 between cysteines 267 and 310. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
5v1b
Structure name
structure of phd1 in complex with 1,2,4-triazolo-[1,5-a]pyridine
Structure deposition date
2017-03-01
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
12
% buried
88
Peptide accession
Q96KS0
Residue number A
267
Residue number B
310
Peptide name
Prolyl hydroxylase EGLN2

Ligandability

Cysteine 267 of Prolyl hydroxylase EGLN2

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 310 of Prolyl hydroxylase EGLN2

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 hydroxylase EGLN2 between cysteines 192 and 310. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
28
PDB code
5v1b
Structure name
structure of phd1 in complex with 1,2,4-triazolo-[1,5-a]pyridine
Structure deposition date
2017-03-01
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
13
% buried
88
Peptide accession
Q96KS0
Residue number A
192
Residue number B
310
Peptide name
Prolyl hydroxylase EGLN2

Ligandability

Cysteine 192 of Prolyl hydroxylase EGLN2

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 310 of Prolyl hydroxylase EGLN2

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 hydroxylase EGLN2 between cysteines 307 and 310. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
28
PDB code
5v1b
Structure name
structure of phd1 in complex with 1,2,4-triazolo-[1,5-a]pyridine
Structure deposition date
2017-03-01
Thiol separation (Å)
9
Half-sphere exposure sum ?
80
Minimum pKa ?
13
% buried
98
Peptide accession
Q96KS0
Residue number A
307
Residue number B
310
Peptide name
Prolyl hydroxylase EGLN2

Ligandability

Cysteine 307 of Prolyl hydroxylase EGLN2

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 310 of Prolyl hydroxylase EGLN2

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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