Serine/threonine-protein kinase MARK1

Intermolecular

Intramolecular

A redox-regulated disulphide may form between two units of Serine/threonine-protein kinase MARK1 at cysteines 217 and 217 (210 and 210 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

2hak

Structure name

catalytic and ubiqutin-associated domains of mark1/par-1

Structure deposition date

2006-06-13

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide A name

Serine/threonine-protein kinase MARK1

Peptide B name

Serine/threonine-protein kinase MARK1

Peptide A accession

Q9P0L2

Peptide B accession

Q9P0L2

Peptide A residue number

217

Peptide B residue number

217

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.

A redox-regulated disulphide may form within Serine/threonine-protein kinase MARK1 between cysteines 730 and 742. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?