Thioredoxin-dependent peroxide reductase, mitochondrial

Intermolecular

A redox-regulated disulphide is known to form between two units of Thioredoxin-dependent peroxide reductase, mitochondrial at cysteines 230 and 109 (168 and 47 respectively in this structure).

Details

Redox score ?

PDB code

4mh3

Structure name

crystal structure of bovine mitochondrial peroxiredoxin iii

Structure deposition date

2013-08-29

Thiol separation (Å)

Half-sphere exposure sum ?

nan

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Thioredoxin-dependent peroxide reductase, mitochondrial

Peptide B name

Thioredoxin-dependent peroxide reductase, mitochondrial

Peptide A accession

P35705

Peptide B accession

P35705

Peptide A residue number

230

Peptide B residue number

109

Ligandability

Cysteine 230 of Thioredoxin-dependent peroxide reductase, mitochondrial

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.

Cysteine 109 of Thioredoxin-dependent peroxide reductase, mitochondrial

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 Thioredoxin-dependent peroxide reductase, mitochondrial at cysteines 60 and 60 (78 and 78 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?