UDP-N-acetylhexosamine pyrophosphorylase

Intramolecular

A redox-regulated disulphide may form within UDP-N-acetylhexosamine pyrophosphorylase between cysteines 268 and 275. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

1jvg

Structure name

crystal structure of human agx2 complexed with udpgalnac

Structure deposition date

2001-08-30

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

100

Peptide accession

Q16222

Residue number A

268

Residue number B

275

Peptide name

UDP-N-acetylhexosamine pyrophosphorylase

Ligandability

Cysteine 268 of UDP-N-acetylhexosamine pyrophosphorylase

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 275 of UDP-N-acetylhexosamine pyrophosphorylase

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 UDP-N-acetylhexosamine pyrophosphorylase between cysteines 431 and 481. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?