Kelch-like protein 12

Intramolecular

A redox-regulated disulphide may form within Kelch-like protein 12 between cysteines 511 and 558. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

6ttk

Structure name

crystal structure of the kelch domain of human klhl12 in complex with dvl1 peptide

Structure deposition date

2019-12-27

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Q53G59

Residue number A

511

Residue number B

558

Peptide name

Kelch-like protein 12

Ligandability

Cysteine 511 of Kelch-like protein 12

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.