Nucleotide triphosphate diphosphatase NUDT15

Intermolecular

Intramolecular

A redox-regulated disulphide may form between two units of Nucleotide triphosphate diphosphatase NUDT15 at cysteines 23 and 59. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

5bon

Structure name

crystal structure of human nudt15 (mth2)

Structure deposition date

2015-05-27

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide A name

Nucleotide triphosphate diphosphatase NUDT15

Peptide B name

Nucleotide triphosphate diphosphatase NUDT15

Peptide A accession

Q9NV35

Peptide B accession

Q9NV35

Peptide A residue number

Peptide B residue number

Ligandability

Cysteine 23 of Nucleotide triphosphate diphosphatase NUDT15

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 59 of Nucleotide triphosphate diphosphatase NUDT15

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 Nucleotide triphosphate diphosphatase NUDT15 between cysteines 59 and 140 (139 and 140 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?