Acyl-coenzyme A thioesterase 11

Intramolecular

A redox-regulated disulphide may form within Acyl-coenzyme A thioesterase 11 between cysteines 529 and 533. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

6vvq

Structure name

human start domain of acyl-coenzyme a thioesterase 11 (acot11) bound to myristic acid

Structure deposition date

2020-02-18

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Q8WXI4

Residue number A

529

Residue number B

533

Peptide name

Acyl-coenzyme A thioesterase 11

Ligandability

Cysteine 529 of Acyl-coenzyme A thioesterase 11

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.