ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Cytochrome P450 2C8

Intramolecular
Cysteine 175 and cysteine 179
Cysteine 164 and cysteine 486
Cysteine 216 and cysteine 225
Cysteine 172 and cysteine 175
Cysteine 172 and cysteine 179
A redox-regulated disulphide may form within Cytochrome P450 2C8 between cysteines 175 and 179.

Details

Redox score ?
62
PDB code
1pq2
Structure name
crystal structure of human drug metabolizing cytochrome p450 2c8
Structure deposition date
2003-06-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
83
Minimum pKa ?
9
% buried
100
Peptide accession
P10632
Residue number A
175
Residue number B
179
Peptide name
Cytochrome P450 2C8

Ligandability

Cysteine 175 of Cytochrome P450 2C8

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 179 of Cytochrome P450 2C8

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 Cytochrome P450 2C8 between cysteines 164 and 486. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
2vn0
Structure name
cyp2c8dh complexed with troglitazone
Structure deposition date
2008-01-30
Thiol separation (Å)
7
Half-sphere exposure sum ?
53
Minimum pKa ?
10
% buried
27
Peptide accession
P10632
Residue number A
164
Residue number B
486
Peptide name
Cytochrome P450 2C8

Ligandability

Cysteine 164 of Cytochrome P450 2C8

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 486 of Cytochrome P450 2C8

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 Cytochrome P450 2C8 between cysteines 216 and 225. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
2nni
Structure name
cyp2c8dh complexed with montelukast
Structure deposition date
2006-10-24
Thiol separation (Å)
8
Half-sphere exposure sum ?
41
Minimum pKa ?
9
% buried
17
Peptide accession
P10632
Residue number A
216
Residue number B
225
Peptide name
Cytochrome P450 2C8

Ligandability

Cysteine 216 of Cytochrome P450 2C8

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 225 of Cytochrome P450 2C8

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 Cytochrome P450 2C8 between cysteines 172 and 175. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
2vn0
Structure name
cyp2c8dh complexed with troglitazone
Structure deposition date
2008-01-30
Thiol separation (Å)
7
Half-sphere exposure sum ?
90
Minimum pKa ?
12
% buried
90
Peptide accession
P10632
Residue number A
172
Residue number B
175
Peptide name
Cytochrome P450 2C8

Ligandability

Cysteine 172 of Cytochrome P450 2C8

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 175 of Cytochrome P450 2C8

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 Cytochrome P450 2C8 between cysteines 172 and 179. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
1pq2
Structure name
crystal structure of human drug metabolizing cytochrome p450 2c8
Structure deposition date
2003-06-17
Thiol separation (Å)
10
Half-sphere exposure sum ?
82
Minimum pKa ?
9
% buried
88
Peptide accession
P10632
Residue number A
172
Residue number B
179
Peptide name
Cytochrome P450 2C8

Ligandability

Cysteine 172 of Cytochrome P450 2C8

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 179 of Cytochrome P450 2C8

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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