Ubiquitin-like modifier-activating enzyme 1

Intramolecular

A redox-regulated disulphide may form within Ubiquitin-like modifier-activating enzyme 1 between cysteines 262 and 278. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

2lzj

Structure name

refined solution structure and dynamics of first catalytic cysteine half-domain from mouse e1 enzyme

Structure deposition date

2012-10-03

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Q02053

Residue number A

262

Residue number B

278

Peptide name

Ubiquitin-like modifier-activating enzyme 1

Ligandability

Cysteine 262 of Ubiquitin-like modifier-activating enzyme 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.

Ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 278 of Ubiquitin-like modifier-activating enzyme 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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Ubiquitin-like modifier-activating enzyme 1 between cysteines 1039 and 1040. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?