a tool for identifying drug-targetable redox-active disulphides

Histone H3.2

Intermolecular

Cysteine 111 and cysteine 111 L

A redox-regulated disulphide may form between two units of Histone H3.2 at cysteines 111 and 111 (110 and 110 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 nucleosome containing histone h3 with the crotonylated lysine 122

Structure deposition date

2015-11-13

Thiol separation (Å)

6

Half-sphere exposure sum ?

79

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

111

Peptide B residue number

111

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.

Ligandable in the dataset of Kuljanin et al.

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