ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Bifunctional epoxide hydrolase 2

Intramolecular
Cysteine 262 and cysteine 264
Cysteine 71 and cysteine 74
Cysteine 309 and cysteine 314
Cysteine 264 and cysteine 314
A redox-regulated disulphide may form within Bifunctional epoxide hydrolase 2 between cysteines 262 and 264.

Details

Redox score ?
60
PDB code
4c4y
Structure name
crystal structure of human bifunctional epoxide hydroxylase 2 complexed with a4
Structure deposition date
2013-09-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
95
Minimum pKa ?
9
% buried
100
Peptide accession
P34913
Residue number A
262
Residue number B
264
Peptide name
Bifunctional epoxide hydrolase 2

Ligandability

Cysteine 262 of Bifunctional epoxide hydrolase 2

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 264 of Bifunctional epoxide hydrolase 2

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 Bifunctional epoxide hydrolase 2 between cysteines 71 and 74. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
5ak6
Structure name
ligand complex structure of soluble epoxide hydrolase
Structure deposition date
2015-03-02
Thiol separation (Å)
8
Half-sphere exposure sum ?
52
Minimum pKa ?
10
% buried
20
Peptide accession
P34913
Residue number A
71
Residue number B
74
Peptide name
Bifunctional epoxide hydrolase 2

Ligandability

Cysteine 71 of Bifunctional epoxide hydrolase 2

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 74 of Bifunctional epoxide hydrolase 2

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 Bifunctional epoxide hydrolase 2 between cysteines 309 and 314. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
6hgw
Structure name
soluble epoxide hydrolase in complex with 2-(4-fluorophenyl)-n-(4- phenoxybenzyl)ethanamine
Structure deposition date
2018-08-23
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
10
% buried
78
Peptide accession
P34913
Residue number A
309
Residue number B
314
Peptide name
Bifunctional epoxide hydrolase 2

Ligandability

Cysteine 309 of Bifunctional epoxide hydrolase 2

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 314 of Bifunctional epoxide hydrolase 2

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 Bifunctional epoxide hydrolase 2 between cysteines 264 and 314. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
29
PDB code
3koo
Structure name
crystal structure of soluble epoxide hydrolase
Structure deposition date
2009-11-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
83
Minimum pKa ?
13
% buried
100
Peptide accession
P34913
Residue number A
264
Residue number B
314
Peptide name
Bifunctional epoxide hydrolase 2

Ligandability

Cysteine 264 of Bifunctional epoxide hydrolase 2

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 314 of Bifunctional epoxide hydrolase 2

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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