a tool for identifying drug-targetable redox-active disulphides

Histone H3.3C

Intermolecular

Cysteine 110 and cysteine 110

A redox-regulated disulphide may form between two units of Histone H3.3C at cysteines 110 and 110 (109 and 109 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

45

PDB code

Structure name

the nucleosome containing human h3

Structure deposition date

2015-04-03

Thiol separation (Å)

6

Half-sphere exposure sum ?

83

Minimum pK_a ?

13

% buried

100

Peptide A name

Histone H3

Peptide B name

Histone H3

Peptide A accession

Peptide B accession

Peptide A residue number

110

Peptide B residue number

110

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.

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