Endophilin-B1

Intermolecular

A redox-regulated disulphide may form between two units of Endophilin-B1 at cysteines 241 and 241. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

6up6

Structure name

endophilin b1 helical scaffold

Structure deposition date

2019-10-16

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide A name

Endophilin-B1

Peptide B name

Endophilin-B1

Peptide A accession

Q9Y371

Peptide B accession

Q9Y371

Peptide A residue number

241

Peptide B residue number

241

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 between two units of Endophilin-B1 at cysteines 121 and 226. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?