a tool for identifying drug-targetable redox-active disulphides

Periphilin-1

Intramolecular

Cysteine 309 and cysteine 352 L

A redox-regulated disulphide may form within Periphilin-1 between cysteines 309 and 352 (316 and 352 respectively in this structure). 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 the tasor-periphilin core complex

Structure deposition date

2019-09-20

Thiol separation (Å)

8

Half-sphere exposure sum ?

64

Minimum pK_a ?

11

% buried

51

Peptide accession

Residue number A

309

Residue number B

352

Peptide name

Periphilin-1

Ligandability

Cysteine 309 of Periphilin-1

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.

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 352 of Periphilin-1

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 352 in protein B could not be asigned to a Uniprot residue.

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