Ribosomal protein S6 kinase alpha-1

Intermolecular

Intramolecular

A redox-regulated disulphide may form between two units of Ribosomal protein S6 kinase alpha-1 at cysteines 575 and 575.

Details

Redox score ?

PDB code

2wnt

Structure name

crystal structure of the human ribosomal protein s6 kinase

Structure deposition date

2009-07-20

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Ribosomal protein S6 kinase alpha-1

Peptide B name

Ribosomal protein S6 kinase alpha-1

Peptide A accession

Q15418

Peptide B accession

Q15418

Peptide A residue number

575

Peptide B residue number

575

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 Ribosomal protein S6 kinase alpha-1 between cysteines 432 and 435. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

2wnt

Structure name

crystal structure of the human ribosomal protein s6 kinase

Structure deposition date

2009-07-20

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Q15418

Residue number A

432

Residue number B

435

Peptide name

Ribosomal protein S6 kinase alpha-1

Ligandability

Cysteine 432 of Ribosomal protein S6 kinase alpha-1

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.

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 435 of Ribosomal protein S6 kinase alpha-1

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 Ribosomal protein S6 kinase alpha-1 between cysteines 432 and 556. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?