Intersectin 2

Intramolecular

A redox-regulated disulphide may form within Intersectin 2 between cysteines 1566 and 1592. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

3jzy

Structure name

crystal structure of human intersectin 2 c2 domain

Structure deposition date

2009-09-24

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

A6H8W8

Residue number A

1566

Residue number B

1592

Peptide name

Intersectin 2

Ligandability

Cysteine 1566 of Intersectin 2

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 1592 of Intersectin 2

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 Intersectin 2 between cysteines 1277 and 1361. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

3gf9

Structure name

crystal structure of human intersectin 2 rhogef domain

Structure deposition date

2009-02-26

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

A6H8W8

Residue number A

1277

Residue number B

1361

Peptide name

Intersectin 2

Ligandability

Cysteine 1277 of Intersectin 2

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 1361 of Intersectin 2

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 Intersectin 2 between cysteines 1277 and 1279. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?