Serine/threonine-protein kinase/endoribonuclease IRE1

Intermolecular

Intramolecular

A redox-regulated disulphide may form between two units of Serine/threonine-protein kinase/endoribonuclease IRE1 at cysteines 630 and 630. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

6w39

Structure name

structure of unphosphorylated ire1 in complex with g-1749

Structure deposition date

2020-03-09

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

100

Peptide A name

Serine/threonine-protein kinase/endoribonuclease IRE1

Peptide B name

Serine/threonine-protein kinase/endoribonuclease IRE1

Peptide A accession

O75460

Peptide B accession

O75460

Peptide A residue number

630

Peptide B residue number

630

Ligandability

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 between two units of Serine/threonine-protein kinase/endoribonuclease IRE1 at cysteines 605 and 605. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

3p23

Structure name

crystal structure of the human kinase and rnase domains in complex with adp

Structure deposition date

2010-10-01

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide A name

Serine/threonine-protein kinase/endoribonuclease IRE1

Peptide B name

Serine/threonine-protein kinase/endoribonuclease IRE1

Peptide A accession

O75460

Peptide B accession

O75460

Peptide A residue number

605

Peptide B residue number

605

Ligandability

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 Serine/threonine-protein kinase/endoribonuclease IRE1 between cysteines 762 and 790. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

7bmk

Structure name

atp-competitive partial antagonists-'pair's-rheostatically modulate ire1alpha's kinase helix-alphac to segregate its rnase-mediated biological outputs

Structure deposition date

2021-01-20

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

O75460

Residue number A

762

Residue number B

790