a tool for identifying drug-targetable redox-active disulphides

FACT complex subunit SPT16

Intramolecular

Cysteine 242 and cysteine 283

A redox-regulated disulphide may form within FACT complex subunit SPT16 between cysteines 242 and 283.

Details

Redox score ?

70

PDB code

Structure name

crystal structure of human spt16 n-terminal domain

Structure deposition date

2015-10-08

Thiol separation (Å)

4

Half-sphere exposure sum ?

84

Minimum pK_a ?

8

% buried

100

Peptide accession

Residue number A

242

Residue number B

283

Peptide name

FACT complex subunit SPT16

Ligandability

Cysteine 242 of FACT complex subunit SPT16

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 283 of FACT complex subunit SPT16

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.

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