Anaphase-promoting complex subunit 1
Intermolecular
Cysteine 36 of Anaphase-promoting complex subunit 10 and cysteine 1288
Intramolecular
Cysteine 443 and cysteine 454
Cysteine 129 and cysteine 152
Cysteine 129 and cysteine 150
Cysteine 225 and cysteine 408
Cysteine 150 and cysteine 152
Cysteine 1469 and cysteine 1487
Cysteine 1755 and cysteine 1778
Cysteine 621 and cysteine 663
Cysteine 962 and cysteine 975
More...Cysteine 1469 and cysteine 1515
Cysteine 1412 and cysteine 1469
7qe7 L 36 A 1288
A redox-regulated disulphide may form between cysteine 36 of Anaphase-promoting complex subunit 10 and cysteine 1288 of Anaphase-promoting complex subunit 1. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
55
PDB code
7qe7
Structure name
high-resolution structure of the anaphase-promoting complex/cyclosome (apc/c) bound to co-activator cdh1
Structure deposition date
2021-12-01
Thiol separation (Å)
7
Half-sphere exposure sum ?
63
Minimum pKa ?
10
% buried
64
Peptide A name
Anaphase-promoting complex subunit 10
Peptide B name
Anaphase-promoting complex subunit 1
Peptide A accession
Q9UM13
Peptide B accession
Q9H1A4
Peptide A residue number
36
Peptide B residue number
1288
Ligandability
Cysteine 36 of Anaphase-promoting complex subunit 10
Cysteine 1288 of Anaphase-promoting complex subunit 1
5lgg A 443 A 454
A redox-regulated disulphide may form within Anaphase-promoting complex subunit 1 between cysteines 443 and 454.
Details
Redox score ?
72
PDB code
5lgg
Structure name
the n-terminal wd40 domain of apc1 (anaphase promoting complex subunit 1)
Structure deposition date
2016-07-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
81
Minimum pKa ?
9
% buried
94
Peptide accession
Q9H1A4
Residue number A
443
Residue number B
454
Peptide name
Anaphase-promoting complex subunit 1
Ligandability
Cysteine 443 of Anaphase-promoting complex subunit 1
Cysteine 454 of Anaphase-promoting complex subunit 1
5lgg A 129 A 152
A redox-regulated disulphide may form within Anaphase-promoting complex subunit 1 between cysteines 129 and 152.
Details
Redox score ?
63
PDB code
5lgg
Structure name
the n-terminal wd40 domain of apc1 (anaphase promoting complex subunit 1)
Structure deposition date
2016-07-07
Thiol separation (Å)
5
Half-sphere exposure sum ?
73
Minimum pKa ?
9
% buried
98
Peptide accession
Q9H1A4
Residue number A
129
Residue number B
152
Peptide name
Anaphase-promoting complex subunit 1
Ligandability
Cysteine 129 of Anaphase-promoting complex subunit 1
Cysteine 152 of Anaphase-promoting complex subunit 1
5lgg A 129 A 150
A redox-regulated disulphide may form within Anaphase-promoting complex subunit 1 between cysteines 129 and 150. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
58
PDB code
5lgg
Structure name
the n-terminal wd40 domain of apc1 (anaphase promoting complex subunit 1)
Structure deposition date
2016-07-07
Thiol separation (Å)
5
Half-sphere exposure sum ?
63
Minimum pKa ?
14
% buried
74
Peptide accession
Q9H1A4
Residue number A
129
Residue number B
150
Peptide name
Anaphase-promoting complex subunit 1
Ligandability
Cysteine 129 of Anaphase-promoting complex subunit 1
Cysteine 150 of Anaphase-promoting complex subunit 1
5lgg A 225 A 408
A redox-regulated disulphide may form within Anaphase-promoting complex subunit 1 between cysteines 225 and 408. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
5lgg
Structure name
the n-terminal wd40 domain of apc1 (anaphase promoting complex subunit 1)
Structure deposition date
2016-07-07
Thiol separation (Å)
7
Half-sphere exposure sum ?
73
Minimum pKa ?
11
% buried
59
Peptide accession
Q9H1A4
Residue number A
225
Residue number B
408
Peptide name
Anaphase-promoting complex subunit 1
Ligandability
Cysteine 225 of Anaphase-promoting complex subunit 1
Cysteine 408 of Anaphase-promoting complex subunit 1
5lgg A 150 A 152
A redox-regulated disulphide may form within Anaphase-promoting complex subunit 1 between cysteines 150 and 152. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
5lgg
Structure name
the n-terminal wd40 domain of apc1 (anaphase promoting complex subunit 1)
Structure deposition date
2016-07-07
Thiol separation (Å)
8
Half-sphere exposure sum ?
69
Minimum pKa ?
9
% buried
76
Peptide accession
Q9H1A4
Residue number A
150
Residue number B
152
Peptide name
Anaphase-promoting complex subunit 1
Ligandability
Cysteine 150 of Anaphase-promoting complex subunit 1
Cysteine 152 of Anaphase-promoting complex subunit 1
7qe7 A 1469 A 1487
A redox-regulated disulphide may form within Anaphase-promoting complex subunit 1 between cysteines 1469 and 1487. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
7qe7
Structure name
high-resolution structure of the anaphase-promoting complex/cyclosome (apc/c) bound to co-activator cdh1
Structure deposition date
2021-12-01
Thiol separation (Å)
7
Half-sphere exposure sum ?
86
Minimum pKa ?
12
% buried
92
Peptide accession
Q9H1A4
Residue number A
1469
Residue number B
1487
Peptide name
Anaphase-promoting complex subunit 1
Ligandability
Cysteine 1469 of Anaphase-promoting complex subunit 1
Cysteine 1487 of Anaphase-promoting complex subunit 1
6tlj A 1755 A 1778
A redox-regulated disulphide may form within Anaphase-promoting complex subunit 1 between cysteines 1755 and 1778. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
35
PDB code
6tlj
Structure name
cryo-em structure of the anaphase-promoting complex/cyclosome, in complex with the mitotic checkpoint complex (apc/c-mcc) at 3
Structure deposition date
2019-12-02
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
12
% buried
92
Peptide accession
Q9H1A4
Residue number A
1755
Residue number B
1778
Peptide name
Anaphase-promoting complex subunit 1
Ligandability
Cysteine 1755 of Anaphase-promoting complex subunit 1
Cysteine 1778 of Anaphase-promoting complex subunit 1
5g04 A 621 A 663
A redox-regulated disulphide may form within Anaphase-promoting complex subunit 1 between cysteines 621 and 663. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
32
PDB code
5g04
Structure name
structure of the human apc-cdc20-hsl1 complex
Structure deposition date
2016-03-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
70
Minimum pKa ?
13
% buried
92
Peptide accession
Q9H1A4
Residue number A
621
Residue number B
663
Peptide name
Anaphase-promoting complex subunit 1
Ligandability
Cysteine 621 of Anaphase-promoting complex subunit 1
Cysteine 663 of Anaphase-promoting complex subunit 1
6tnt A 962 A 975
A redox-regulated disulphide may form within Anaphase-promoting complex subunit 1 between cysteines 962 and 975. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
32
PDB code
6tnt
Structure name
sumoylated apoapc/c with repositioned apc2 whb domain
Structure deposition date
2019-12-10
Thiol separation (Å)
10
Half-sphere exposure sum ?
70
Minimum pKa ?
11
% buried
79
Peptide accession
Q9H1A4
Residue number A
962
Residue number B
975
Peptide name
Anaphase-promoting complex subunit 1
Ligandability
Cysteine 962 of Anaphase-promoting complex subunit 1
Cysteine 975 of Anaphase-promoting complex subunit 1
6tnt A 1469 A 1515
A redox-regulated disulphide may form within Anaphase-promoting complex subunit 1 between cysteines 1469 and 1515. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
29
PDB code
6tnt
Structure name
sumoylated apoapc/c with repositioned apc2 whb domain
Structure deposition date
2019-12-10
Thiol separation (Å)
8
Half-sphere exposure sum ?
101
Minimum pKa ?
13
% buried
100
Peptide accession
Q9H1A4
Residue number A
1469
Residue number B
1515
Peptide name
Anaphase-promoting complex subunit 1
Ligandability
Cysteine 1469 of Anaphase-promoting complex subunit 1
Cysteine 1515 of Anaphase-promoting complex subunit 1
5g04 A 1412 A 1469
A redox-regulated disulphide may form within Anaphase-promoting complex subunit 1 between cysteines 1412 and 1469. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
21
PDB code
5g04
Structure name
structure of the human apc-cdc20-hsl1 complex
Structure deposition date
2016-03-16
Thiol separation (Å)
10
Half-sphere exposure sum ?
104
Minimum pKa ?
11
% buried
100
Peptide accession
Q9H1A4
Residue number A
1412
Residue number B
1469
Peptide name
Anaphase-promoting complex subunit 1
Ligandability
Cysteine 1412 of Anaphase-promoting complex subunit 1
Cysteine 1469 of Anaphase-promoting complex subunit 1
If this tool was useful for finding a disulphide, please cite: