Proteasome subunit alpha type-6
Intramolecular
Cysteine 115 and cysteine 154 L
Cysteine 137 and cysteine 154 L
Cysteine 136 and cysteine 137
Cysteine 136 and cysteine 154 L
Cysteine 78 and cysteine 154 L
Cysteine 115 and cysteine 161
Cysteine 115 and cysteine 137
Cysteine 137 and cysteine 161
Cysteine 78 and cysteine 115
Cysteine 78 and cysteine 137
More...Cysteine 154 and cysteine 161 L
Cysteine 78 and cysteine 136
6tu3 O 115 O 154
A redox-regulated disulphide may form within Proteasome subunit alpha type-6 between cysteines 115 and 154.
Details
Redox score ?
70
PDB code
6tu3
Structure name
rat 20s proteasome
Structure deposition date
2020-01-02
Thiol separation (Å)
3
Half-sphere exposure sum ?
81
Minimum pKa ?
9
% buried
100
Peptide accession
P60901
Residue number A
115
Residue number B
154
Peptide name
Proteasome subunit alpha type-6
Ligandability
Cysteine 115 of Proteasome subunit alpha type-6
Cysteine 154 of Proteasome subunit alpha type-6
3une w 137 w 154
A redox-regulated disulphide may form within Proteasome subunit alpha type-6 between cysteines 137 and 154. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
54
PDB code
3une
Structure name
mouse constitutive 20s proteasome
Structure deposition date
2011-11-15
Thiol separation (Å)
6
Half-sphere exposure sum ?
94
Minimum pKa ?
8
% buried
100
Peptide accession
Q9QUM9
Residue number A
137
Residue number B
154
Peptide name
Proteasome subunit alpha type-6
Ligandability
Cysteine 137 of Proteasome subunit alpha type-6
Cysteine 154 of Proteasome subunit alpha type-6
7dr6 L 136 L 137
A redox-regulated disulphide may form within Proteasome subunit alpha type-6 between cysteines 136 and 137. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
7dr6
Structure name
pa28alpha-beta in complex with immunoproteasome
Structure deposition date
2020-12-26
Thiol separation (Å)
7
Half-sphere exposure sum ?
90
Minimum pKa ?
10
% buried
100
Peptide accession
Q2YDE4
Residue number A
136
Residue number B
137
Peptide name
Proteasome subunit alpha type-6
Ligandability
Cysteine 136 of Proteasome subunit alpha type-6
Cysteine 137 of Proteasome subunit alpha type-6
6epe A 136 A 154
A redox-regulated disulphide may form within Proteasome subunit alpha type-6 between cysteines 136 and 154. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
6epe
Structure name
substrate processing state 26s proteasome (sps2)
Structure deposition date
2017-10-11
Thiol separation (Å)
7
Half-sphere exposure sum ?
98
Minimum pKa ?
11
% buried
100
Peptide accession
P60901
Residue number A
136
Residue number B
154
Peptide name
Proteasome subunit alpha type-6
Ligandability
Cysteine 136 of Proteasome subunit alpha type-6
Cysteine 154 of Proteasome subunit alpha type-6
6epf A 78 A 154
A redox-regulated disulphide may form within Proteasome subunit alpha type-6 between cysteines 78 and 154. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
6epf
Structure name
ground state 26s proteasome (gs1)
Structure deposition date
2017-10-11
Thiol separation (Å)
8
Half-sphere exposure sum ?
99
Minimum pKa ?
9
% buried
100
Peptide accession
P60901
Residue number A
78
Residue number B
154
Peptide name
Proteasome subunit alpha type-6
Ligandability
Cysteine 78 of Proteasome subunit alpha type-6
Cysteine 154 of Proteasome subunit alpha type-6
3unb i 114 i 160
A redox-regulated disulphide may form within Proteasome subunit alpha type-6 between cysteines 115 and 161 (114 and 160 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
35
PDB code
3unb
Structure name
mouse constitutive 20s proteasome in complex with pr-957
Structure deposition date
2011-11-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
81
Minimum pKa ?
11
% buried
92
Peptide accession
Q9QUM9
Residue number A
115
Residue number B
161
Peptide name
Proteasome subunit alpha type-6
Ligandability
Cysteine 115 of Proteasome subunit alpha type-6
Cysteine 161 of Proteasome subunit alpha type-6
3une w 115 w 137
A redox-regulated disulphide may form within Proteasome subunit alpha type-6 between cysteines 115 and 137. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
32
PDB code
3une
Structure name
mouse constitutive 20s proteasome
Structure deposition date
2011-11-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
96
Minimum pKa ?
12
% buried
100
Peptide accession
Q9QUM9
Residue number A
115
Residue number B
137
Peptide name
Proteasome subunit alpha type-6
Ligandability
Cysteine 115 of Proteasome subunit alpha type-6
Cysteine 137 of Proteasome subunit alpha type-6
5a0q O 137 O 161
A redox-regulated disulphide may form within Proteasome subunit alpha type-6 between cysteines 137 and 161. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
32
PDB code
5a0q
Structure name
cryo-em reveals the conformation of a substrate analogue in the human 20s proteasome core
Structure deposition date
2015-04-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
87
Minimum pKa ?
11
% buried
96
Peptide accession
P60900
Residue number A
137
Residue number B
161
Peptide name
Proteasome subunit alpha type-6
Ligandability
Cysteine 137 of Proteasome subunit alpha type-6
Cysteine 161 of Proteasome subunit alpha type-6
7dr7 E 78 E 115
A redox-regulated disulphide may form within Proteasome subunit alpha type-6 between cysteines 78 and 115. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
31
PDB code
7dr7
Structure name
bovine 20s immunoproteasome
Structure deposition date
2020-12-26
Thiol separation (Å)
8
Half-sphere exposure sum ?
94
Minimum pKa ?
13
% buried
100
Peptide accession
Q2YDE4
Residue number A
78
Residue number B
115
Peptide name
Proteasome subunit alpha type-6
Ligandability
Cysteine 78 of Proteasome subunit alpha type-6
Cysteine 115 of Proteasome subunit alpha type-6
6xmj A 78 A 137
A redox-regulated disulphide may form within Proteasome subunit alpha type-6 between cysteines 78 and 137. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
29
PDB code
6xmj
Structure name
human 20s proteasome bound to an engineered 11s (pa26) activator
Structure deposition date
2020-06-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
100
Minimum pKa ?
12
% buried
100
Peptide accession
P60900
Residue number A
78
Residue number B
137
Peptide name
Proteasome subunit alpha type-6
Ligandability
Cysteine 78 of Proteasome subunit alpha type-6
Cysteine 137 of Proteasome subunit alpha type-6
6epe A 154 A 161
A redox-regulated disulphide may form within Proteasome subunit alpha type-6 between cysteines 154 and 161. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
26
PDB code
6epe
Structure name
substrate processing state 26s proteasome (sps2)
Structure deposition date
2017-10-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
91
Minimum pKa ?
11
% buried
100
Peptide accession
P60901
Residue number A
154
Residue number B
161
Peptide name
Proteasome subunit alpha type-6
Ligandability
Cysteine 154 of Proteasome subunit alpha type-6
Cysteine 161 of Proteasome subunit alpha type-6
7dr6 e 78 e 136
A redox-regulated disulphide may form within Proteasome subunit alpha type-6 between cysteines 78 and 136. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
25
PDB code
7dr6
Structure name
pa28alpha-beta in complex with immunoproteasome
Structure deposition date
2020-12-26
Thiol separation (Å)
9
Half-sphere exposure sum ?
87
Minimum pKa ?
13
% buried
100
Peptide accession
Q2YDE4
Residue number A
78
Residue number B
136
Peptide name
Proteasome subunit alpha type-6
Ligandability
Cysteine 78 of Proteasome subunit alpha type-6
Cysteine 136 of Proteasome subunit alpha type-6
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