Heat shock protein HSP 90-beta

Intermolecular

Intramolecular

A redox-regulated disulphide may form between two units of Heat shock protein HSP 90-beta at cysteines 366 and 366. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

8eob

Structure name

cryo-em structure of human hsp90b in the closed state

Structure deposition date

2022-10-02

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide A name

Heat shock protein HSP 90-beta

Peptide B name

Heat shock protein HSP 90-beta

Peptide A accession

P08238

Peptide B accession

P08238

Peptide A residue number

366

Peptide B residue number

366

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 Heat shock protein HSP 90-beta between cysteines 564 and 589. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

8h77

Structure name

hsp90-ahr-p23-xap2 complex

Structure deposition date

2022-10-19

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

P11499

Residue number A

564

Residue number B

589

Peptide name

Heat shock protein HSP 90-beta

Ligandability

Cysteine 564 of Heat shock protein HSP 90-beta

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 589 of Heat shock protein HSP 90-beta

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 Heat shock protein HSP 90-beta between cysteines 589 and 590. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?