ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Peroxisomal multifunctional enzyme type 2

Intermolecular
Cysteine 277 and cysteine 230
Intramolecular
Cysteine 425 and cysteine 455
Cysteine 226 and cysteine 230
Cysteine 373 and cysteine 455
Cysteine 189 and cysteine 226
A redox-regulated disulphide may form between two units of Peroxisomal multifunctional enzyme type 2 at cysteines 277 and 230. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
1zbq
Structure name
crystal structure of human 17-beta-hydroxysteroid dehydrogenase type 4 in complex with nad
Structure deposition date
2005-04-08
Thiol separation (Å)
9
Half-sphere exposure sum ?
59
Minimum pKa ?
12
% buried
74
Peptide A name
Peroxisomal multifunctional enzyme type 2
Peptide B name
Peroxisomal multifunctional enzyme type 2
Peptide A accession
P51659
Peptide B accession
P51659
Peptide A residue number
277
Peptide B residue number
230

Ligandability

Cysteine 277 of Peroxisomal multifunctional enzyme type 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 230 of Peroxisomal multifunctional enzyme type 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 Peroxisomal multifunctional enzyme type 2 between cysteines 425 and 455 (108 and 138 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
1s9c
Structure name
crystal structure analysis of the 2-enoyl-coa hydratase 2 domain of human peroxisomal multifunctional enzyme type 2
Structure deposition date
2004-02-04
Thiol separation (Å)
7
Half-sphere exposure sum ?
73
Minimum pKa ?
11
% buried
79
Peptide accession
P51659
Residue number A
425
Residue number B
455
Peptide name
Peroxisomal multifunctional enzyme type 2

Ligandability

Cysteine 425 of Peroxisomal multifunctional enzyme type 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 455 of Peroxisomal multifunctional enzyme type 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 Peroxisomal multifunctional enzyme type 2 between cysteines 226 and 230. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
1gz6
Structure name
(3r)-hydroxyacyl-coa dehydrogenase fragment of rat peroxisomal multifunctional enzyme type 2
Structure deposition date
2002-05-16
Thiol separation (Å)
8
Half-sphere exposure sum ?
74
Minimum pKa ?
12
% buried
97
Peptide accession
P97852
Residue number A
226
Residue number B
230
Peptide name
Peroxisomal multifunctional enzyme type 2

Ligandability

Cysteine 226 of Peroxisomal multifunctional enzyme type 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 230 of Peroxisomal multifunctional enzyme type 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 Peroxisomal multifunctional enzyme type 2 between cysteines 373 and 455 (56 and 138 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
29
PDB code
1s9c
Structure name
crystal structure analysis of the 2-enoyl-coa hydratase 2 domain of human peroxisomal multifunctional enzyme type 2
Structure deposition date
2004-02-04
Thiol separation (Å)
10
Half-sphere exposure sum ?
79
Minimum pKa ?
12
% buried
97
Peptide accession
P51659
Residue number A
373
Residue number B
455
Peptide name
Peroxisomal multifunctional enzyme type 2

Ligandability

Cysteine 373 of Peroxisomal multifunctional enzyme type 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 455 of Peroxisomal multifunctional enzyme type 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 Peroxisomal multifunctional enzyme type 2 between cysteines 189 and 226. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
28
PDB code
1gz6
Structure name
(3r)-hydroxyacyl-coa dehydrogenase fragment of rat peroxisomal multifunctional enzyme type 2
Structure deposition date
2002-05-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
87
Minimum pKa ?
13
% buried
100
Peptide accession
P97852
Residue number A
189
Residue number B
226
Peptide name
Peroxisomal multifunctional enzyme type 2

Ligandability

Cysteine 189 of Peroxisomal multifunctional enzyme type 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 226 of Peroxisomal multifunctional enzyme type 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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