G1/S-specific cyclin-D3

A redox-regulated disulphide may form within G1/S-specific cyclin-D3 between cysteines 189 and 243. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

7sj3

Structure name

structure of cdk4-cyclin d3 bound to abemaciclib

Structure deposition date

2021-10-15

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

P30281

Residue number A

189

Residue number B

243

Peptide name

G1/S-specific cyclin-D3

Ligandability

Cysteine 189 of G1/S-specific cyclin-D3

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 243 of G1/S-specific cyclin-D3

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 G1/S-specific cyclin-D3 between cysteines 239 and 243. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

3g33

Structure name

crystal structure of cdk4/cyclin d3

Structure deposition date

2009-02-01

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Q6FG62

Residue number A

239

Residue number B

243

Peptide name

G1/S-specific cyclin-D3

Ligandability

Cysteine 239 of G1/S-specific cyclin-D3

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 243 of G1/S-specific cyclin-D3

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 G1/S-specific cyclin-D3 between cysteines 47 and 91. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?