Cullin-5

Intermolecular

Intramolecular

A redox-regulated disulphide may form between two units of Cullin-5 at cysteines 188 and 188. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

4n9f

Structure name

crystal structure of the vif-cbfbeta-cul5-elob-eloc pentameric complex

Structure deposition date

2013-10-21

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide A name

Cullin-5

Peptide B name

Cullin-5

Peptide A accession

Q93034

Peptide B accession

Q93034

Peptide A residue number

188

Peptide B residue number

188

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 Cullin-5 between cysteines 264 and 265.

Details

Redox score ?

PDB code

4n9f

Structure name

crystal structure of the vif-cbfbeta-cul5-elob-eloc pentameric complex

Structure deposition date

2013-10-21

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Q93034

Residue number A

264

Residue number B

265

Peptide name

Cullin-5

Ligandability

Cysteine 264 of Cullin-5

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 265 of Cullin-5

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 Cullin-5 between cysteines 51 and 112. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?