ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Proteasome (Prosome, macropain) 26S subunit, non-ATPase, 12

Intramolecular
Cysteine 108 and cysteine 109
Cysteine 74 and cysteine 108
Cysteine 74 and cysteine 109
A redox-regulated disulphide may form within Proteasome (Prosome, macropain) 26S subunit, non-ATPase, 12 between cysteines 108 and 109. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
6epc
Structure name
ground state 26s proteasome (gs2)
Structure deposition date
2017-10-11
Thiol separation (Å)
6
Half-sphere exposure sum ?
84
Minimum pKa ?
12
% buried
100
Peptide accession
Q5XIC6
Residue number A
108
Residue number B
109
Peptide name
Proteasome (Prosome, macropain) 26S subunit, non-ATPase, 12

Ligandability

Cysteine 108 of Proteasome (Prosome, macropain) 26S subunit, non-ATPase, 12

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 109 of Proteasome (Prosome, macropain) 26S subunit, non-ATPase, 12

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 (Prosome, macropain) 26S subunit, non-ATPase, 12 between cysteines 74 and 108. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
6epd
Structure name
substrate processing state 26s proteasome (sps1)
Structure deposition date
2017-10-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
78
Minimum pKa ?
7
% buried
81
Peptide accession
Q5XIC6
Residue number A
74
Residue number B
108
Peptide name
Proteasome (Prosome, macropain) 26S subunit, non-ATPase, 12

Ligandability

Cysteine 74 of Proteasome (Prosome, macropain) 26S subunit, non-ATPase, 12

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 108 of Proteasome (Prosome, macropain) 26S subunit, non-ATPase, 12

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 (Prosome, macropain) 26S subunit, non-ATPase, 12 between cysteines 74 and 109. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
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 ?
77
Minimum pKa ?
11
% buried
62
Peptide accession
Q5XIC6
Residue number A
74
Residue number B
109
Peptide name
Proteasome (Prosome, macropain) 26S subunit, non-ATPase, 12

Ligandability

Cysteine 74 of Proteasome (Prosome, macropain) 26S subunit, non-ATPase, 12

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 109 of Proteasome (Prosome, macropain) 26S subunit, non-ATPase, 12

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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