ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Isocitrate dehydrogenase [NADP] cytoplasmic

Intramolecular
Cysteine 132 and cysteine 269 L
Cysteine 269 and cysteine 269 L
Cysteine 114 and cysteine 379 L
A redox-regulated disulphide may form within Isocitrate dehydrogenase [NADP] cytoplasmic between cysteines 132 and 269.

Details

Redox score ?
75
PDB code
6io0
Structure name
human idh1 r132c mutant complexed with compound a
Structure deposition date
2018-10-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
7
% buried
85
Peptide accession
O75874
Residue number A
132
Residue number B
269
Peptide name
Isocitrate dehydrogenase [NADP] cytoplasmic

Ligandability

Cysteine 132 of Isocitrate dehydrogenase [NADP] cytoplasmic

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 269 of Isocitrate dehydrogenase [NADP] cytoplasmic

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Ligandable in the dataset of Backus et al.

Ligandable in the dataset of Vinogradova et al.

Ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

Cysteine 132 in protein A could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within Isocitrate dehydrogenase [NADP] cytoplasmic between cysteines 269 and 269 (132 and 269 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
8bay
Structure name
crystal structure of idh1 variant r132c s280f in complex with nadph, ca2+ and 3-butyl-2-oxoglutarate
Structure deposition date
2022-10-12
Thiol separation (Å)
7
Half-sphere exposure sum ?
87
Minimum pKa ?
11
% buried
100
Peptide accession
O75874
Residue number A
269
Residue number B
269
Peptide name
Isocitrate dehydrogenase [NADP] cytoplasmic

Ligandability

Cysteine 269 of Isocitrate dehydrogenase [NADP] cytoplasmic

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Ligandable in the dataset of Backus et al.

Ligandable in the dataset of Vinogradova et al.

Ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

Cysteine 269 of Isocitrate dehydrogenase [NADP] cytoplasmic

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Ligandable in the dataset of Backus et al.

Ligandable in the dataset of Vinogradova et al.

Ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Isocitrate dehydrogenase [NADP] cytoplasmic between cysteines 114 and 379. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
4l03
Structure name
crystal structure analysis of human idh1 mutants in complex with nadp+ and ca2+/alpha-ketoglutarate
Structure deposition date
2013-05-30
Thiol separation (Å)
10
Half-sphere exposure sum ?
65
Minimum pKa ?
12
% buried
78
Peptide accession
O75874
Residue number A
114
Residue number B
379
Peptide name
Isocitrate dehydrogenase [NADP] cytoplasmic

Ligandability

Cysteine 114 of Isocitrate dehydrogenase [NADP] cytoplasmic

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 379 of Isocitrate dehydrogenase [NADP] cytoplasmic

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.

Ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

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