a tool for identifying drug-targetable redox-active disulphides

Inosine-5'-monophosphate dehydrogenase 2

Intermolecular

Cysteine 26 and cysteine 26

Cysteine 339 and cysteine 468 L

Intramolecular

Cysteine 327 and cysteine 331 L

Cysteine 331 and cysteine 339 L

A redox-regulated disulphide may form between two units of Inosine-5'-monophosphate dehydrogenase 2 at cysteines 26 and 26. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

38

PDB code

Structure name

human impdh2 treated with atp, imp, nad+, and 2 mm gtp

Structure deposition date

2019-09-10

Thiol separation (Å)

10

Half-sphere exposure sum ?

50

Minimum pK_a ?

10

% buried

46

Peptide A name

Inosine-5'-monophosphate dehydrogenase 2

Peptide B name

Inosine-5'-monophosphate dehydrogenase 2

Peptide A accession

Peptide B accession

Peptide A residue number

26

Peptide B residue number

26

Ligandability

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 between two units of Inosine-5'-monophosphate dehydrogenase 2 at cysteines 339 and 468. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

21

PDB code

Structure name

human impdh2 treated with atp, imp, nad+, and 2 mm gtp

Structure deposition date

2019-09-10

Thiol separation (Å)

10

Half-sphere exposure sum ?

96

Minimum pK_a ?

12

% buried

94

Peptide A name

Inosine-5'-monophosphate dehydrogenase 2

Peptide B name

Inosine-5'-monophosphate dehydrogenase 2

Peptide A accession

Peptide B accession

Peptide A residue number

339

Peptide B residue number

468

Ligandability

Cysteine 339 of Inosine-5'-monophosphate dehydrogenase 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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 468 of Inosine-5'-monophosphate dehydrogenase 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 Inosine-5'-monophosphate dehydrogenase 2 between cysteines 327 and 331. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

46

PDB code

Structure name

crystal structure of inosine monophosphate dehydrogenase in complex with mycophenolic acid

Structure deposition date

2001-08-09

Thiol separation (Å)

7

Half-sphere exposure sum ?

70

Minimum pK_a ?

10

% buried

84

Peptide accession

Residue number A

327

Residue number B

331

Peptide name

Inosine-5'-monophosphate dehydrogenase 2

Ligandability

Cysteine 327 of Inosine-5'-monophosphate dehydrogenase 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 331 of Inosine-5'-monophosphate dehydrogenase 2

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.

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.

A redox-regulated disulphide may form within Inosine-5'-monophosphate dehydrogenase 2 between cysteines 331 and 339. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

25

PDB code

Structure name

human impdh2 treated with atp, imp, nad+, and 2 mm gtp

Structure deposition date

2019-09-10

Thiol separation (Å)

10

Half-sphere exposure sum ?

92

Minimum pK_a ?

11

% buried

100

Peptide accession

Residue number A

331

Residue number B

339

Peptide name

Inosine-5'-monophosphate dehydrogenase 2

Ligandability

Cysteine 331 of Inosine-5'-monophosphate dehydrogenase 2

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.

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 339 of Inosine-5'-monophosphate dehydrogenase 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.

Ligandable in the dataset of Kuljanin et al.

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