ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

26S proteasome regulatory subunit 6A

Intramolecular
Cysteine 396 and cysteine 400 L
Cysteine 387 and cysteine 396 L
A redox-regulated disulphide may form within 26S proteasome regulatory subunit 6A between cysteines 396 and 400. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
5ln3
Structure name
the human 26s proteasome at 6
Structure deposition date
2016-08-03
Thiol separation (Å)
7
Half-sphere exposure sum ?
88
Minimum pKa ?
11
% buried
92
Peptide accession
P17980
Residue number A
396
Residue number B
400
Peptide name
26S proteasome regulatory subunit 6A

Ligandability

Cysteine 396 of 26S proteasome regulatory subunit 6A

Cysteine 400 of 26S proteasome regulatory subunit 6A

A redox-regulated disulphide may form within 26S proteasome regulatory subunit 6A between cysteines 387 and 396. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
PDB code
5gjq
Structure name
structure of the human 26s proteasome bound to usp14-ubal
Structure deposition date
2016-07-01
Thiol separation (Å)
10
Half-sphere exposure sum ?
82
Minimum pKa ?
12
% buried
92
Peptide accession
P17980
Residue number A
387
Residue number B
396
Peptide name
26S proteasome regulatory subunit 6A

Ligandability

Cysteine 387 of 26S proteasome regulatory subunit 6A

Cysteine 396 of 26S proteasome regulatory subunit 6A

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