Bifunctional purine biosynthesis protein ATIC

Intramolecular

A redox-regulated disulphide may form within Bifunctional purine biosynthesis protein ATIC between cysteines 101 and 146. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

5uy8

Structure name

crystal structure of aicarft bound to an antifolate

Structure deposition date

2017-02-23

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

100

Peptide accession

P31939

Residue number A

101

Residue number B

146

Peptide name

Bifunctional purine biosynthesis protein ATIC

Ligandability

Cysteine 101 of Bifunctional purine biosynthesis protein ATIC

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 146 of Bifunctional purine biosynthesis protein ATIC

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 Bifunctional purine biosynthesis protein ATIC between cysteines 434 and 454. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?