ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Proteasome subunit beta type-1

Intramolecular
Cysteine 70 and cysteine 223
Cysteine 81 and cysteine 88
Cysteine 71 and cysteine 89
Cysteine 70 and cysteine 81
A redox-regulated disulphide may form within Proteasome subunit beta type-1 between cysteines 70 and 223 (43 and 196 respectively in this structure).

Details

Redox score ?
77
PDB code
3unb
Structure name
mouse constitutive 20s proteasome in complex with pr-957
Structure deposition date
2011-11-15
Thiol separation (Å)
3
Half-sphere exposure sum ?
84
Minimum pKa ?
7
% buried
80
Peptide accession
O09061
Residue number A
70
Residue number B
223
Peptide name
Proteasome subunit beta type-1

Ligandability

Cysteine 70 of Proteasome subunit beta type-1

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 223 of Proteasome subunit beta type-1

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-1 between cysteines 81 and 88 (54 and 61 respectively in this structure).

Details

Redox score ?
76
PDB code
3une
Structure name
mouse constitutive 20s proteasome
Structure deposition date
2011-11-15
Thiol separation (Å)
2
Half-sphere exposure sum ?
90
Minimum pKa ?
nan
% buried
nan
Peptide accession
O09061
Residue number A
81
Residue number B
88
Peptide name
Proteasome subunit beta type-1

Ligandability

Cysteine 81 of Proteasome subunit beta type-1

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 88 of Proteasome subunit beta type-1

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-1 between cysteines 71 and 89. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
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 ?
70
Minimum pKa ?
11
% buried
90
Peptide accession
P20618
Residue number A
71
Residue number B
89
Peptide name
Proteasome subunit beta type-1

Ligandability

Cysteine 71 of Proteasome subunit beta type-1

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 89 of Proteasome subunit beta type-1

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-1 between cysteines 70 and 81 (43 and 54 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
25
PDB code
6tu3
Structure name
rat 20s proteasome
Structure deposition date
2020-01-02
Thiol separation (Å)
8
Half-sphere exposure sum ?
85
Minimum pKa ?
17
% buried
100
Peptide accession
P18421
Residue number A
70
Residue number B
81
Peptide name
Proteasome subunit beta type-1

Ligandability

Cysteine 70 of Proteasome subunit beta type-1

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 81 of Proteasome subunit beta type-1

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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