Proteasome subunit alpha type-4
5lf4 B 34 B 163
A redox-regulated disulphide may form within Proteasome subunit alpha type-4 between cysteines 34 and 163. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
5lf4
Structure name
human 20s proteasome complex with delanzomib at 2
Structure deposition date
2016-06-30
Thiol separation (Å)
7
Half-sphere exposure sum ?
100
Minimum pKa ?
11
% buried
98
Peptide accession
P25789
Residue number A
34
Residue number B
163
Peptide name
Proteasome subunit alpha type-4
Ligandability
Cysteine 34 of Proteasome subunit alpha type-4
Cysteine 163 of Proteasome subunit alpha type-4
6epf C 34 C 74
A redox-regulated disulphide may form within Proteasome subunit alpha type-4 between cysteines 34 and 74. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
35
PDB code
6epf
Structure name
ground state 26s proteasome (gs1)
Structure deposition date
2017-10-11
Thiol separation (Å)
8
Half-sphere exposure sum ?
101
Minimum pKa ?
12
% buried
100
Peptide accession
P21670
Residue number A
34
Residue number B
74
Peptide name
Proteasome subunit alpha type-4
Ligandability
Cysteine 34 of Proteasome subunit alpha type-4
Cysteine 74 of Proteasome subunit alpha type-4
5ln3 C 74 C 107
A redox-regulated disulphide may form within Proteasome subunit alpha type-4 between cysteines 74 and 107. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
31
PDB code
5ln3
Structure name
the human 26s proteasome at 6
Structure deposition date
2016-08-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
83
Minimum pKa ?
12
% buried
94
Peptide accession
P25789
Residue number A
74
Residue number B
107
Peptide name
Proteasome subunit alpha type-4
Ligandability
Cysteine 74 of Proteasome subunit alpha type-4
Cysteine 107 of Proteasome subunit alpha type-4
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