ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Proteasome subunit beta type-3

Intermolecular
Cysteine 74 of Proteasome subunit beta type-7 and cysteine 129
Cysteine 247 of Proteasome subunit beta type-7 and cysteine 150
Cysteine 70 of Proteasome subunit beta type-10 and cysteine 129
Intramolecular
Cysteine 122 and cysteine 129
Cysteine 142 and cysteine 150
A redox-regulated disulphide may form between cysteine 74 of Proteasome subunit beta type-7 and cysteine 129 of Proteasome subunit beta type-3 (31 and 128 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
3unb
Structure name
mouse constitutive 20s proteasome in complex with pr-957
Structure deposition date
2011-11-15
Thiol separation (Å)
6
Half-sphere exposure sum ?
72
Minimum pKa ?
14
% buried
100
Peptide A name
Proteasome subunit beta type-7
Peptide B name
Proteasome subunit beta type-3
Peptide A accession
P70195
Peptide B accession
Q9R1P1
Peptide A residue number
74
Peptide B residue number
129

Ligandability

Cysteine 74 of Proteasome subunit beta type-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 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 between cysteine 247 of Proteasome subunit beta type-7 and cysteine 150 of Proteasome subunit beta type-3 (204 and 149 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
5a0q
Structure name
cryo-em reveals the conformation of a substrate analogue in the human 20s proteasome core
Structure deposition date
2015-04-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
11
% buried
80
Peptide A name
Proteasome subunit beta type-7
Peptide B name
Proteasome subunit beta type-3
Peptide A accession
Q99436
Peptide B accession
P49720
Peptide A residue number
247
Peptide B residue number
150

Ligandability

Cysteine 247 of Proteasome subunit beta type-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 150 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 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-3 between cysteines 122 and 129. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
25
PDB code
5ln3
Structure name
the human 26s proteasome at 6
Structure deposition date
2016-08-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
73
Minimum pKa ?
12
% buried
76
Peptide accession
P49720
Residue number A
122
Residue number B
129
Peptide name
Proteasome subunit beta type-3

Ligandability

Cysteine 122 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.

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-3 between cysteines 142 and 150. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
25
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)
10
Half-sphere exposure sum ?
86
Minimum pKa ?
13
% buried
100
Peptide accession
P49720
Residue number A
142
Residue number B
150
Peptide name
Proteasome subunit beta type-3

Ligandability

Cysteine 142 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.

Cysteine 150 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.

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