ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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26S proteasome regulatory subunit 7

Intramolecular
Cysteine 236 and cysteine 270 L
Cysteine 180 and cysteine 225
Cysteine 377 and cysteine 389 L
A redox-regulated disulphide may form within 26S proteasome regulatory subunit 7 between cysteines 236 and 270. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
59
PDB code
5t0j
Structure name
structural basis for dynamic regulation of the human 26s proteasome
Structure deposition date
2016-08-16
Thiol separation (Å)
7
Half-sphere exposure sum ?
53
Minimum pKa ?
9
% buried
22
Peptide accession
P35998
Residue number A
236
Residue number B
270
Peptide name
26S proteasome regulatory subunit 7

Ligandability

Cysteine 236 of 26S proteasome regulatory subunit 7

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.

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 270 of 26S proteasome regulatory subunit 7

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 26S proteasome regulatory subunit 7 between cysteines 180 and 225. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
5m32
Structure name
human 26s proteasome in complex with oprozomib
Structure deposition date
2016-10-14
Thiol separation (Å)
6
Half-sphere exposure sum ?
76
Minimum pKa ?
10
% buried
92
Peptide accession
P35998
Residue number A
180
Residue number B
225
Peptide name
26S proteasome regulatory subunit 7

Ligandability

Cysteine 180 of 26S proteasome regulatory subunit 7

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.

Cysteine 225 of 26S proteasome regulatory subunit 7

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 26S proteasome regulatory subunit 7 between cysteines 377 and 389. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
5vhs
Structure name
conformational landscape of the p28-bound human proteasome regulatory particle
Structure deposition date
2017-04-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
68
Minimum pKa ?
10
% buried
74
Peptide accession
P35998
Residue number A
377
Residue number B
389
Peptide name
26S proteasome regulatory subunit 7

Ligandability

Cysteine 377 of 26S proteasome regulatory subunit 7

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.

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 389 of 26S proteasome regulatory subunit 7

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.

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