ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Alkyldihydroxyacetonephosphate synthase, peroxisomal

Intramolecular
Cysteine 541 and cysteine 565
Cysteine 231 and cysteine 247
Cysteine 404 and cysteine 413
A redox-regulated disulphide may form within Alkyldihydroxyacetonephosphate synthase, peroxisomal between cysteines 541 and 565.

Details

Redox score ?
71
PDB code
5ae3
Structure name
ether lipid-generating enzyme agps in complex with antimycin a
Structure deposition date
2015-08-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
81
Minimum pKa ?
8
% buried
100
Peptide accession
P97275
Residue number A
541
Residue number B
565
Peptide name
Alkyldihydroxyacetonephosphate synthase, peroxisomal

Ligandability

Cysteine 541 of Alkyldihydroxyacetonephosphate synthase, peroxisomal

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 565 of Alkyldihydroxyacetonephosphate synthase, peroxisomal

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 Alkyldihydroxyacetonephosphate synthase, peroxisomal between cysteines 231 and 247. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
5ae3
Structure name
ether lipid-generating enzyme agps in complex with antimycin a
Structure deposition date
2015-08-25
Thiol separation (Å)
7
Half-sphere exposure sum ?
81
Minimum pKa ?
12
% buried
98
Peptide accession
P97275
Residue number A
231
Residue number B
247
Peptide name
Alkyldihydroxyacetonephosphate synthase, peroxisomal

Ligandability

Cysteine 231 of Alkyldihydroxyacetonephosphate synthase, peroxisomal

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 247 of Alkyldihydroxyacetonephosphate synthase, peroxisomal

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 Alkyldihydroxyacetonephosphate synthase, peroxisomal between cysteines 404 and 413. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
6gou
Structure name
development of alkyl glycerone phosphate synthase inhibitors: complex with inhibitor 2i
Structure deposition date
2018-06-04
Thiol separation (Å)
9
Half-sphere exposure sum ?
75
Minimum pKa ?
11
% buried
73
Peptide accession
P97275
Residue number A
404
Residue number B
413
Peptide name
Alkyldihydroxyacetonephosphate synthase, peroxisomal

Ligandability

Cysteine 404 of Alkyldihydroxyacetonephosphate synthase, peroxisomal

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 413 of Alkyldihydroxyacetonephosphate synthase, peroxisomal

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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