Thialysine N-epsilon-acetyltransferase

Intermolecular

Intramolecular

A redox-regulated disulphide may form between two units of Thialysine N-epsilon-acetyltransferase at cysteines 158 and 122. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

2q4v

Structure name

ensemble refinement of the protein crystal structure of thialysine n- acetyltransferase (ssat2) from homo sapiens

Structure deposition date

2007-05-31

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide A name

Thialysine N-epsilon-acetyltransferase

Peptide B name

Thialysine N-epsilon-acetyltransferase

Peptide A accession

Q96F10

Peptide B accession

Q96F10

Peptide A residue number

158

Peptide B residue number

122

Ligandability

Cysteine 158 of Thialysine N-epsilon-acetyltransferase

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.

Cysteine 122 of Thialysine N-epsilon-acetyltransferase

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 Thialysine N-epsilon-acetyltransferase between cysteines 14 and 54. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?