N-alpha-acetyltransferase 50

Intramolecular

A redox-regulated disulphide may form within N-alpha-acetyltransferase 50 between cysteines 61 and 100. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

6wfn

Structure name

crystal structure of human naa50 in complex with accoa and an inhibitor (compound 4a) identified using dna encoded library technology

Structure deposition date

2020-04-03

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Q9GZZ1

Residue number A

Residue number B

100

Peptide name

N-alpha-acetyltransferase 50

Ligandability

Cysteine 61 of N-alpha-acetyltransferase 50

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 100 of N-alpha-acetyltransferase 50

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 N-alpha-acetyltransferase 50 between cysteines 60 and 61. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?