THO complex subunit 1

Intermolecular

Cysteine 156 and cysteine 202 of THO complex subunit 2 L

Intramolecular

A redox-regulated disulphide may form between cysteine 156 of THO complex subunit 1 and cysteine 202 of THO complex subunit 2. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

7apk

Structure name

structure of the human tho - uap56 complex

Structure deposition date

2020-10-17

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide A name

THO complex subunit 1

Peptide B name

THO complex subunit 2

Peptide A accession

Q96FV9

Peptide B accession

Q8NI27

Peptide A residue number

156

Peptide B residue number

202

Ligandability

Cysteine 156 of THO complex subunit 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.

Cysteine 202 of THO complex subunit 2

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 THO complex subunit 1 between cysteines 103 and 109. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?