Transaldolase

Intramolecular

A redox-regulated disulphide may form within Transaldolase between cysteines 164 and 178. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

1f05

Structure name

crystal structure of human transaldolase

Structure deposition date

2000-05-14

Thiol separation (Å)

Half-sphere exposure sum ?

100

Minimum pK_a ?

% buried

100

Peptide accession

P37837

Residue number A

164

Residue number B

178

Peptide name

Transaldolase

Ligandability

Cysteine 164 of Transaldolase

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.