ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Proteasome subunit alpha type-1

Intermolecular
Cysteine 156 and cysteine 390 of Proteasome (Prosome, macropain) 26S subunit, ATPase 3
Cysteine 148 and cysteine 390 of Proteasome (Prosome, macropain) 26S subunit, ATPase 3
Intramolecular
Cysteine 85 and cysteine 92
Cysteine 148 and cysteine 156
A redox-regulated disulphide may form between cysteine 156 of Proteasome subunit alpha type-1 and cysteine 390 of Proteasome (Prosome, macropain) 26S subunit, ATPase 3. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
6epc
Structure name
ground state 26s proteasome (gs2)
Structure deposition date
2017-10-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
83
Minimum pKa ?
9
% buried
100
Peptide A name
Proteasome subunit alpha type-1
Peptide B name
Proteasome (Prosome, macropain) 26S subunit, ATPase 3
Peptide A accession
P18420
Peptide B accession
Q6P6U2
Peptide A residue number
156
Peptide B residue number
390

Ligandability

Cysteine 156 of Proteasome subunit alpha 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 390 of Proteasome (Prosome, macropain) 26S subunit, ATPase 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 148 of Proteasome subunit alpha type-1 and cysteine 390 of Proteasome (Prosome, macropain) 26S subunit, ATPase 3. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
6epc
Structure name
ground state 26s proteasome (gs2)
Structure deposition date
2017-10-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
88
Minimum pKa ?
9
% buried
100
Peptide A name
Proteasome subunit alpha type-1
Peptide B name
Proteasome (Prosome, macropain) 26S subunit, ATPase 3
Peptide A accession
P18420
Peptide B accession
Q6P6U2
Peptide A residue number
148
Peptide B residue number
390

Ligandability

Cysteine 148 of Proteasome subunit alpha 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 390 of Proteasome (Prosome, macropain) 26S subunit, ATPase 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 alpha type-1 between cysteines 85 and 92. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
7dr7
Structure name
bovine 20s immunoproteasome
Structure deposition date
2020-12-26
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
11
% buried
98
Peptide accession
Q3T0X5
Residue number A
85
Residue number B
92
Peptide name
Proteasome subunit alpha type-1

Ligandability

Cysteine 85 of Proteasome subunit alpha 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 92 of Proteasome subunit alpha 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 alpha type-1 between cysteines 148 and 156. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
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)
9
Half-sphere exposure sum ?
81
Minimum pKa ?
11
% buried
100
Peptide accession
P25786
Residue number A
148
Residue number B
156
Peptide name
Proteasome subunit alpha type-1

Ligandability

Cysteine 148 of Proteasome subunit alpha 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 156 of Proteasome subunit alpha 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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