Lysine (K)-specific demethylase 2A

Intermolecular

Intramolecular

A redox-regulated disulphide may form between two units of Lysine (K)-specific demethylase 2A at cysteines 333 and 477. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

4qx7

Structure name

crystal structure of histone demethylase kdm2a-h3k36me2 with alpha-kg

Structure deposition date

2014-07-18

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide A name

Lysine (K)-specific demethylase 2A

Peptide B name

Lysine (K)-specific demethylase 2A

Peptide A accession

F6YRW4

Peptide B accession

F6YRW4

Peptide A residue number

333

Peptide B residue number

477

Ligandability

Cysteine 333 of Lysine (K)-specific demethylase 2A

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 477 of Lysine (K)-specific demethylase 2A

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 within Lysine (K)-specific demethylase 2A between cysteines 101 and 200. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?