Proteasome activator complex subunit 4
Intramolecular
Cysteine 637 and cysteine 638
Cysteine 1000 and cysteine 1001 L
Cysteine 519 and cysteine 537
Cysteine 1227 and cysteine 1232
Cysteine 1001 and cysteine 1048 L
Cysteine 650 and cysteine 651
Cysteine 637 and cysteine 737
Cysteine 500 and cysteine 554
Cysteine 638 and cysteine 737
Cysteine 718 and cysteine 820
More...Cysteine 597 and cysteine 638
Cysteine 1001 and cysteine 1039 L
Cysteine 958 and cysteine 1000
Cysteine 597 and cysteine 637
Cysteine 631 and cysteine 650
Cysteine 1000 and cysteine 1048
Cysteine 597 and cysteine 737
Cysteine 1427 and cysteine 1432
Cysteine 1732 and cysteine 1769
6kwx A 637 A 638
A redox-regulated disulphide may form within Proteasome activator complex subunit 4 between cysteines 637 and 638.
Details
Redox score ?
62
PDB code
6kwx
Structure name
cryo-em structure of human pa200
Structure deposition date
2019-09-09
Thiol separation (Å)
5
Half-sphere exposure sum ?
77
Minimum pKa ?
9
% buried
86
Peptide accession
Q14997
Residue number A
637
Residue number B
638
Peptide name
Proteasome activator complex subunit 4
Ligandability
Cysteine 637 of Proteasome activator complex subunit 4
Cysteine 638 of Proteasome activator complex subunit 4
8cvs c 1000 c 1001
A redox-regulated disulphide may form within Proteasome activator complex subunit 4 between cysteines 1000 and 1001. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
58
PDB code
8cvs
Structure name
human pa200-20s proteasome with mg-132
Structure deposition date
2022-05-18
Thiol separation (Å)
5
Half-sphere exposure sum ?
77
Minimum pKa ?
11
% buried
86
Peptide accession
Q14997
Residue number A
1000
Residue number B
1001
Peptide name
Proteasome activator complex subunit 4
Ligandability
Cysteine 1000 of Proteasome activator complex subunit 4
Cysteine 1001 of Proteasome activator complex subunit 4
6kwy c 519 c 537
A redox-regulated disulphide may form within Proteasome activator complex subunit 4 between cysteines 519 and 537. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
58
PDB code
6kwy
Structure name
human pa200-20s complex
Structure deposition date
2019-09-09
Thiol separation (Å)
6
Half-sphere exposure sum ?
71
Minimum pKa ?
10
% buried
33
Peptide accession
Q14997
Residue number A
519
Residue number B
537
Peptide name
Proteasome activator complex subunit 4
Ligandability
Cysteine 519 of Proteasome activator complex subunit 4
Cysteine 537 of Proteasome activator complex subunit 4
6rey c 1227 c 1232
A redox-regulated disulphide may form within Proteasome activator complex subunit 4 between cysteines 1227 and 1232. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
6rey
Structure name
human 20s-pa200 proteasome complex
Structure deposition date
2019-04-12
Thiol separation (Å)
9
Half-sphere exposure sum ?
32
Minimum pKa ?
9
% buried
0
Peptide accession
Q14997
Residue number A
1227
Residue number B
1232
Peptide name
Proteasome activator complex subunit 4
Ligandability
Cysteine 1227 of Proteasome activator complex subunit 4
Cysteine 1232 of Proteasome activator complex subunit 4
8cvs c 1001 c 1048
A redox-regulated disulphide may form within Proteasome activator complex subunit 4 between cysteines 1001 and 1048. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
8cvs
Structure name
human pa200-20s proteasome with mg-132
Structure deposition date
2022-05-18
Thiol separation (Å)
8
Half-sphere exposure sum ?
70
Minimum pKa ?
11
% buried
80
Peptide accession
Q14997
Residue number A
1001
Residue number B
1048
Peptide name
Proteasome activator complex subunit 4
Ligandability
Cysteine 1001 of Proteasome activator complex subunit 4
Cysteine 1048 of Proteasome activator complex subunit 4
8cvs c 650 c 651
A redox-regulated disulphide may form within Proteasome activator complex subunit 4 between cysteines 650 and 651. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
8cvs
Structure name
human pa200-20s proteasome with mg-132
Structure deposition date
2022-05-18
Thiol separation (Å)
7
Half-sphere exposure sum ?
74
Minimum pKa ?
12
% buried
90
Peptide accession
Q14997
Residue number A
650
Residue number B
651
Peptide name
Proteasome activator complex subunit 4
Ligandability
Cysteine 650 of Proteasome activator complex subunit 4
Cysteine 651 of Proteasome activator complex subunit 4
8cvs c 637 c 737
A redox-regulated disulphide may form within Proteasome activator complex subunit 4 between cysteines 637 and 737. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
8cvs
Structure name
human pa200-20s proteasome with mg-132
Structure deposition date
2022-05-18
Thiol separation (Å)
7
Half-sphere exposure sum ?
78
Minimum pKa ?
11
% buried
90
Peptide accession
Q14997
Residue number A
637
Residue number B
737
Peptide name
Proteasome activator complex subunit 4
Ligandability
Cysteine 637 of Proteasome activator complex subunit 4
Cysteine 737 of Proteasome activator complex subunit 4
6kwx A 500 A 554
A redox-regulated disulphide may form within Proteasome activator complex subunit 4 between cysteines 500 and 554. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
6kwx
Structure name
cryo-em structure of human pa200
Structure deposition date
2019-09-09
Thiol separation (Å)
7
Half-sphere exposure sum ?
74
Minimum pKa ?
11
% buried
84
Peptide accession
Q14997
Residue number A
500
Residue number B
554
Peptide name
Proteasome activator complex subunit 4
Ligandability
Cysteine 500 of Proteasome activator complex subunit 4
Cysteine 554 of Proteasome activator complex subunit 4
8cvs c 638 c 737
A redox-regulated disulphide may form within Proteasome activator complex subunit 4 between cysteines 638 and 737. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
8cvs
Structure name
human pa200-20s proteasome with mg-132
Structure deposition date
2022-05-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
75
Minimum pKa ?
8
% buried
74
Peptide accession
Q14997
Residue number A
638
Residue number B
737
Peptide name
Proteasome activator complex subunit 4
Ligandability
Cysteine 638 of Proteasome activator complex subunit 4
Cysteine 737 of Proteasome activator complex subunit 4
8cvs c 718 c 820
A redox-regulated disulphide may form within Proteasome activator complex subunit 4 between cysteines 718 and 820. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
8cvs
Structure name
human pa200-20s proteasome with mg-132
Structure deposition date
2022-05-18
Thiol separation (Å)
7
Half-sphere exposure sum ?
88
Minimum pKa ?
12
% buried
99
Peptide accession
Q14997
Residue number A
718
Residue number B
820
Peptide name
Proteasome activator complex subunit 4
Ligandability
Cysteine 718 of Proteasome activator complex subunit 4
Cysteine 820 of Proteasome activator complex subunit 4
8cvs c 597 c 638
A redox-regulated disulphide may form within Proteasome activator complex subunit 4 between cysteines 597 and 638. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
36
PDB code
8cvs
Structure name
human pa200-20s proteasome with mg-132
Structure deposition date
2022-05-18
Thiol separation (Å)
10
Half-sphere exposure sum ?
77
Minimum pKa ?
8
% buried
80
Peptide accession
Q14997
Residue number A
597
Residue number B
638
Peptide name
Proteasome activator complex subunit 4
Ligandability
Cysteine 597 of Proteasome activator complex subunit 4
Cysteine 638 of Proteasome activator complex subunit 4
6kwx A 1001 A 1039
A redox-regulated disulphide may form within Proteasome activator complex subunit 4 between cysteines 1001 and 1039. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
36
PDB code
6kwx
Structure name
cryo-em structure of human pa200
Structure deposition date
2019-09-09
Thiol separation (Å)
10
Half-sphere exposure sum ?
76
Minimum pKa ?
8
% buried
88
Peptide accession
Q14997
Residue number A
1001
Residue number B
1039
Peptide name
Proteasome activator complex subunit 4
Ligandability
Cysteine 1001 of Proteasome activator complex subunit 4
Cysteine 1039 of Proteasome activator complex subunit 4
6kwx A 958 A 1000
A redox-regulated disulphide may form within Proteasome activator complex subunit 4 between cysteines 958 and 1000. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
36
PDB code
6kwx
Structure name
cryo-em structure of human pa200
Structure deposition date
2019-09-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
11
% buried
83
Peptide accession
Q14997
Residue number A
958
Residue number B
1000
Peptide name
Proteasome activator complex subunit 4
Ligandability
Cysteine 958 of Proteasome activator complex subunit 4
Cysteine 1000 of Proteasome activator complex subunit 4
6rey d 597 d 637
A redox-regulated disulphide may form within Proteasome activator complex subunit 4 between cysteines 597 and 637. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
36
PDB code
6rey
Structure name
human 20s-pa200 proteasome complex
Structure deposition date
2019-04-12
Thiol separation (Å)
8
Half-sphere exposure sum ?
81
Minimum pKa ?
12
% buried
94
Peptide accession
Q14997
Residue number A
597
Residue number B
637
Peptide name
Proteasome activator complex subunit 4
Ligandability
Cysteine 597 of Proteasome activator complex subunit 4
Cysteine 637 of Proteasome activator complex subunit 4
6kwx A 631 A 650
A redox-regulated disulphide may form within Proteasome activator complex subunit 4 between cysteines 631 and 650. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
36
PDB code
6kwx
Structure name
cryo-em structure of human pa200
Structure deposition date
2019-09-09
Thiol separation (Å)
8
Half-sphere exposure sum ?
83
Minimum pKa ?
13
% buried
100
Peptide accession
Q14997
Residue number A
631
Residue number B
650
Peptide name
Proteasome activator complex subunit 4
Ligandability
Cysteine 631 of Proteasome activator complex subunit 4
Cysteine 650 of Proteasome activator complex subunit 4
6rey c 1000 c 1048
A redox-regulated disulphide may form within Proteasome activator complex subunit 4 between cysteines 1000 and 1048. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
6rey
Structure name
human 20s-pa200 proteasome complex
Structure deposition date
2019-04-12
Thiol separation (Å)
10
Half-sphere exposure sum ?
67
Minimum pKa ?
11
% buried
76
Peptide accession
Q14997
Residue number A
1000
Residue number B
1048
Peptide name
Proteasome activator complex subunit 4
Ligandability
Cysteine 1000 of Proteasome activator complex subunit 4
Cysteine 1048 of Proteasome activator complex subunit 4
6kwx A 597 A 737
A redox-regulated disulphide may form within Proteasome activator complex subunit 4 between cysteines 597 and 737. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
31
PDB code
6kwx
Structure name
cryo-em structure of human pa200
Structure deposition date
2019-09-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
83
Minimum pKa ?
12
% buried
94
Peptide accession
Q14997
Residue number A
597
Residue number B
737
Peptide name
Proteasome activator complex subunit 4
Ligandability
Cysteine 597 of Proteasome activator complex subunit 4
Cysteine 737 of Proteasome activator complex subunit 4
6rey c 1427 c 1432
A redox-regulated disulphide may form within Proteasome activator complex subunit 4 between cysteines 1427 and 1432. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
29
PDB code
6rey
Structure name
human 20s-pa200 proteasome complex
Structure deposition date
2019-04-12
Thiol separation (Å)
10
Half-sphere exposure sum ?
83
Minimum pKa ?
12
% buried
100
Peptide accession
Q14997
Residue number A
1427
Residue number B
1432
Peptide name
Proteasome activator complex subunit 4
Ligandability
Cysteine 1427 of Proteasome activator complex subunit 4
Cysteine 1432 of Proteasome activator complex subunit 4
6kwy c 1732 c 1769
A redox-regulated disulphide may form within Proteasome activator complex subunit 4 between cysteines 1732 and 1769. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
27
PDB code
6kwy
Structure name
human pa200-20s complex
Structure deposition date
2019-09-09
Thiol separation (Å)
10
Half-sphere exposure sum ?
77
Minimum pKa ?
12
% buried
89
Peptide accession
Q14997
Residue number A
1732
Residue number B
1769
Peptide name
Proteasome activator complex subunit 4
Ligandability
Cysteine 1732 of Proteasome activator complex subunit 4
Cysteine 1769 of Proteasome activator complex subunit 4
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