Ran-binding protein 10

A redox-regulated disulphide may form within Ran-binding protein 10 between cysteines 151 and 180. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

5jia

Structure name

the crystal structure of ius-spry domain from ranbp10

Structure deposition date

2016-04-22

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Q6VN19

Residue number A

151

Residue number B

180

Peptide name

Ran-binding protein 10

Ligandability

Cysteine 151 of Ran-binding protein 10

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 180 of Ran-binding protein 10

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 Ran-binding protein 10 between cysteines 172 and 180. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

5jia

Structure name

the crystal structure of ius-spry domain from ranbp10

Structure deposition date

2016-04-22

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

100

Peptide accession

Q6VN19

Residue number A

172

Residue number B

180

Peptide name

Ran-binding protein 10

Ligandability

Cysteine 172 of Ran-binding protein 10

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 180 of Ran-binding protein 10

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 Ran-binding protein 10 between cysteines 171 and 172. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?