ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Proteasome subunit beta type-10

Intermolecular
Cysteine 70 and cysteine 129 of Proteasome subunit beta type-3
Intramolecular
Cysteine 82 and cysteine 83
Cysteine 83 and cysteine 215
Cysteine 82 and cysteine 215
Cysteine 70 and cysteine 83
A redox-regulated disulphide may form between cysteine 70 of Proteasome subunit beta type-10 and cysteine 129 of Proteasome subunit beta type-3 (31 and 129 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
7awe
Structure name
human immunoproteasome 20s particle in complex with [(1r)-2-(1- benzofuran-3-yl)-1-{[(1s,2r,4r)-7-oxabicyclo[2
Structure deposition date
2020-11-06
Thiol separation (Å)
8
Half-sphere exposure sum ?
71
Minimum pKa ?
12
% buried
94
Peptide A name
Proteasome subunit beta type-10
Peptide B name
Proteasome subunit beta type-3
Peptide A accession
P40306
Peptide B accession
P49720
Peptide A residue number
70
Peptide B residue number
129

Ligandability

Cysteine 70 of Proteasome subunit beta type-10

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 129 of Proteasome subunit beta type-3

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 Proteasome subunit beta type-10 between cysteines 82 and 83 (43 and 44 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
3unh
Structure name
mouse 20s immunoproteasome
Structure deposition date
2011-11-15
Thiol separation (Å)
7
Half-sphere exposure sum ?
99
Minimum pKa ?
12
% buried
100
Peptide accession
O35955
Residue number A
82
Residue number B
83
Peptide name
Proteasome subunit beta type-10

Ligandability

Cysteine 82 of Proteasome subunit beta type-10

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 83 of Proteasome subunit beta type-10

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 Proteasome subunit beta type-10 between cysteines 83 and 215 (44 and 176 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
6e5b
Structure name
human immunoproteasome 20s particle in complex with compound 1
Structure deposition date
2018-07-19
Thiol separation (Å)
8
Half-sphere exposure sum ?
94
Minimum pKa ?
12
% buried
87
Peptide accession
P40306
Residue number A
83
Residue number B
215
Peptide name
Proteasome subunit beta type-10

Ligandability

Cysteine 83 of Proteasome subunit beta type-10

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 215 of Proteasome subunit beta type-10

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 Proteasome subunit beta type-10 between cysteines 82 and 215. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
27
PDB code
7dr7
Structure name
bovine 20s immunoproteasome
Structure deposition date
2020-12-26
Thiol separation (Å)
10
Half-sphere exposure sum ?
94
Minimum pKa ?
12
% buried
84
Peptide accession
Q3T0T1
Residue number A
82
Residue number B
215
Peptide name
Proteasome subunit beta type-10

Ligandability

Cysteine 82 of Proteasome subunit beta type-10

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 215 of Proteasome subunit beta type-10

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 Proteasome subunit beta type-10 between cysteines 70 and 83. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
26
PDB code
7drw
Structure name
bovine 20s immunoproteasome in complex with two human pa28alpha-beta activators
Structure deposition date
2020-12-29
Thiol separation (Å)
10
Half-sphere exposure sum ?
81
Minimum pKa ?
11
% buried
89
Peptide accession
Q3T0T1
Residue number A
70
Residue number B
83
Peptide name
Proteasome subunit beta type-10

Ligandability

Cysteine 70 of Proteasome subunit beta type-10

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 83 of Proteasome subunit beta type-10

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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