ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Proteasome subunit alpha type-7

Intramolecular
Cysteine 63 and cysteine 70 L
Cysteine 63 and cysteine 97
Cysteine 70 and cysteine 91 L
A redox-regulated disulphide may form within Proteasome subunit alpha type-7 between cysteines 63 and 70 (62 and 69 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
3unb
Structure name
mouse constitutive 20s proteasome in complex with pr-957
Structure deposition date
2011-11-15
Thiol separation (Å)
8
Half-sphere exposure sum ?
88
Minimum pKa ?
10
% buried
100
Peptide accession
Q9Z2U0
Residue number A
63
Residue number B
70
Peptide name
Proteasome subunit alpha type-7

Ligandability

Cysteine 63 of Proteasome subunit alpha 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 70 of Proteasome subunit alpha 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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Proteasome subunit alpha type-7 between cysteines 63 and 97. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
27
PDB code
6epe
Structure name
substrate processing state 26s proteasome (sps2)
Structure deposition date
2017-10-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
86
Minimum pKa ?
12
% buried
100
Peptide accession
P48004
Residue number A
63
Residue number B
97
Peptide name
Proteasome subunit alpha type-7

Ligandability

Cysteine 63 of Proteasome subunit alpha 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 97 of Proteasome subunit alpha 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.

A redox-regulated disulphide may form within Proteasome subunit alpha type-7 between cysteines 70 and 91. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
23
PDB code
7nao
Structure name
human pa28-20s proteasome complex
Structure deposition date
2021-06-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
86
Minimum pKa ?
13
% buried
95
Peptide accession
O14818
Residue number A
70
Residue number B
91
Peptide name
Proteasome subunit alpha type-7

Ligandability

Cysteine 70 of Proteasome subunit alpha 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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 91 of Proteasome subunit alpha 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.

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