THO complex subunit 5 homolog

Intermolecular

Cysteine 59 and cysteine 60 of THO complex subunit 7 homolog L

Intramolecular

A redox-regulated disulphide may form between cysteine 59 of THO complex subunit 5 homolog and cysteine 60 of THO complex subunit 7 homolog. 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 5 homolog

Peptide B name

THO complex subunit 7 homolog

Peptide A accession

Q13769

Peptide B accession

Q6I9Y2

Peptide A residue number

Peptide B residue number

Ligandability

Cysteine 59 of THO complex subunit 5 homolog

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 60 of THO complex subunit 7 homolog

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 5 homolog between cysteines 507 and 613. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?