Arylamine N-acetyltransferase 1

Intramolecular

A redox-regulated disulphide may form within Arylamine N-acetyltransferase 1 between cysteines 223 and 233. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

2ija

Structure name

human n-acetyltransferase 1 f125s mutant

Structure deposition date

2006-09-29

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

P18440

Residue number A

223

Residue number B

233

Peptide name

Arylamine N-acetyltransferase 1

Ligandability

Cysteine 223 of Arylamine N-acetyltransferase 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.