Intersectin-1

Intermolecular

Intramolecular

A redox-regulated disulphide may form between two units of Intersectin-1 at cysteines 1410 and 1410. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

3jv3

Structure name

structure of sh3e-dh unit of murine intersectin-1l

Structure deposition date

2009-09-15

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide A name

Intersectin-1

Peptide B name

Intersectin-1

Peptide A accession

Q9Z0R4

Peptide B accession

Q9Z0R4

Peptide A residue number

1410

Peptide B residue number

1410

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 Intersectin-1 between cysteines 1333 and 1417 (1476 and 1560 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

5hzj

Structure name

crystal structure of photoinhibitable intersectin1 containing wildtype lov2 domain

Structure deposition date

2016-02-02

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Q15811

Residue number A

1333

Residue number B

1417

Peptide name

Intersectin-1

Ligandability

Cysteine 1333 of Intersectin-1

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 1417 of Intersectin-1

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-1 between cysteines 1326 and 1328. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?