Cyclin-C

Intermolecular

Cysteine 64 of Cyclin-dependent kinase 8 and cysteine 148

Intramolecular

A redox-regulated disulphide may form between cysteine 64 of Cyclin-dependent kinase 8 and cysteine 148 of Cyclin-C. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

5bnj

Structure name

cdk8/cycc in complex with 8-{3-chloro-5-[4-(1-methyl-1h-pyrazol-4-yl)- phenyl]-pyridin- 4-yl}-2,8-diaza-spiro[4

Structure deposition date

2015-05-26

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

100

Peptide A name

Cyclin-dependent kinase 8

Peptide B name

Cyclin-C

Peptide A accession

P49336

Peptide B accession

P24863

Peptide A residue number

Peptide B residue number

148

Ligandability

Cysteine 64 of Cyclin-dependent kinase 8

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 148 of Cyclin-C

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 Cyclin-C between cysteines 90 and 138. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

5hbh

Structure name

cdk8-cycc in complex with 5-{5-chloro-4-[1-(2-methoxy-ethyl)-1,8- diaza-spiro[4

Structure deposition date

2015-12-31

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

100

Peptide accession

P24863

Residue number A

Residue number B

138

Peptide name

Cyclin-C

Ligandability

Cysteine 90 of Cyclin-C

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 138 of Cyclin-C

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 Cyclin-C between cysteines 148 and 149. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?