Anaphase-promoting complex subunit 11
Intramolecular
Cysteine 34 and cysteine 44
Cysteine 34 and cysteine 37
Cysteine 51 and cysteine 76
Cysteine 37 and cysteine 44
Cysteine 23 and cysteine 59
Cysteine 73 and cysteine 76
Cysteine 51 and cysteine 73
Cysteine 23 and cysteine 26
Cysteine 34 and cysteine 59
Cysteine 26 and cysteine 59
More...Cysteine 33 and cysteine 37
Cysteine 33 and cysteine 34
Cysteine 33 and cysteine 44
Cysteine 26 and cysteine 34
Cysteine 23 and cysteine 44
Cysteine 44 and cysteine 59
Cysteine 23 and cysteine 34
Cysteine 23 and cysteine 54
Cysteine 26 and cysteine 44
Cysteine 23 and cysteine 37
Cysteine 26 and cysteine 33
Cysteine 51 and cysteine 54
Cysteine 23 and cysteine 73
Cysteine 37 and cysteine 59
Cysteine 26 and cysteine 37
Cysteine 33 and cysteine 59
Cysteine 54 and cysteine 76
Cysteine 54 and cysteine 73
Cysteine 26 and cysteine 54
Cysteine 44 and cysteine 54
Cysteine 54 and cysteine 59
4r2y C 34 C 44
A redox-regulated disulphide may form within Anaphase-promoting complex subunit 11 between cysteines 34 and 44.
Details
Redox score ?
89
PDB code
4r2y
Structure name
crystal structure of apc11 ring domain
Structure deposition date
2014-08-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
6
% buried
2
Peptide accession
Q9NYG5
Residue number A
34
Residue number B
44
Peptide name
Anaphase-promoting complex subunit 11
Ligandability
Cysteine 34 of Anaphase-promoting complex subunit 11
Cysteine 44 of Anaphase-promoting complex subunit 11
4r2y C 34 C 37
A redox-regulated disulphide may form within Anaphase-promoting complex subunit 11 between cysteines 34 and 37.
Details
Redox score ?
87
PDB code
4r2y
Structure name
crystal structure of apc11 ring domain
Structure deposition date
2014-08-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
6
% buried
1
Peptide accession
Q9NYG5
Residue number A
34
Residue number B
37
Peptide name
Anaphase-promoting complex subunit 11
Ligandability
Cysteine 34 of Anaphase-promoting complex subunit 11
Cysteine 37 of Anaphase-promoting complex subunit 11
5jg6 A 51 A 76
A redox-regulated disulphide may form within Anaphase-promoting complex subunit 11 between cysteines 51 and 76.
Details
Redox score ?
84
PDB code
5jg6
Structure name
apc11-ubv shows role of noncovalent ring-ubiquitin interactions in processive multiubiquitination and ubiquitin chain elongation by apc/c
Structure deposition date
2016-04-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
38
Minimum pKa ?
7
% buried
12
Peptide accession
Q9NYG5
Residue number A
51
Residue number B
76
Peptide name
Anaphase-promoting complex subunit 11
Ligandability
Cysteine 51 of Anaphase-promoting complex subunit 11
Cysteine 76 of Anaphase-promoting complex subunit 11
4r2y C 37 C 44
A redox-regulated disulphide may form within Anaphase-promoting complex subunit 11 between cysteines 37 and 44.
Details
Redox score ?
84
PDB code
4r2y
Structure name
crystal structure of apc11 ring domain
Structure deposition date
2014-08-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
44
Minimum pKa ?
9
% buried
2
Peptide accession
Q9NYG5
Residue number A
37
Residue number B
44
Peptide name
Anaphase-promoting complex subunit 11
Ligandability
Cysteine 37 of Anaphase-promoting complex subunit 11
Cysteine 44 of Anaphase-promoting complex subunit 11
5jg6 A 23 A 59
A redox-regulated disulphide may form within Anaphase-promoting complex subunit 11 between cysteines 23 and 59.
Details
Redox score ?
82
PDB code
5jg6
Structure name
apc11-ubv shows role of noncovalent ring-ubiquitin interactions in processive multiubiquitination and ubiquitin chain elongation by apc/c
Structure deposition date
2016-04-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
6
% buried
32
Peptide accession
Q9NYG5
Residue number A
23
Residue number B
59
Peptide name
Anaphase-promoting complex subunit 11
Ligandability
Cysteine 23 of Anaphase-promoting complex subunit 11
Cysteine 59 of Anaphase-promoting complex subunit 11
5jg6 A 73 A 76
A redox-regulated disulphide may form within Anaphase-promoting complex subunit 11 between cysteines 73 and 76.
Details
Redox score ?
82
PDB code
5jg6
Structure name
apc11-ubv shows role of noncovalent ring-ubiquitin interactions in processive multiubiquitination and ubiquitin chain elongation by apc/c
Structure deposition date
2016-04-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
7
% buried
18
Peptide accession
Q9NYG5
Residue number A
73
Residue number B
76
Peptide name
Anaphase-promoting complex subunit 11
Ligandability
Cysteine 73 of Anaphase-promoting complex subunit 11
Cysteine 76 of Anaphase-promoting complex subunit 11
5jg6 D 51 D 73
A redox-regulated disulphide may form within Anaphase-promoting complex subunit 11 between cysteines 51 and 73.
Details
Redox score ?
78
PDB code
5jg6
Structure name
apc11-ubv shows role of noncovalent ring-ubiquitin interactions in processive multiubiquitination and ubiquitin chain elongation by apc/c
Structure deposition date
2016-04-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
9
% buried
30
Peptide accession
Q9NYG5
Residue number A
51
Residue number B
73
Peptide name
Anaphase-promoting complex subunit 11
Ligandability
Cysteine 51 of Anaphase-promoting complex subunit 11
Cysteine 73 of Anaphase-promoting complex subunit 11
4r2y D 23 D 26
A redox-regulated disulphide may form within Anaphase-promoting complex subunit 11 between cysteines 23 and 26.
Details
Redox score ?
78
PDB code
4r2y
Structure name
crystal structure of apc11 ring domain
Structure deposition date
2014-08-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
8
% buried
nan
Peptide accession
Q9NYG5
Residue number A
23
Residue number B
26
Peptide name
Anaphase-promoting complex subunit 11
Ligandability
Cysteine 23 of Anaphase-promoting complex subunit 11
Cysteine 26 of Anaphase-promoting complex subunit 11
4r2y B 34 B 59
A redox-regulated disulphide may form within Anaphase-promoting complex subunit 11 between cysteines 34 and 59.
Details
Redox score ?
76
PDB code
4r2y
Structure name
crystal structure of apc11 ring domain
Structure deposition date
2014-08-13
Thiol separation (Å)
5
Half-sphere exposure sum ?
67
Minimum pKa ?
6
% buried
40
Peptide accession
Q9NYG5
Residue number A
34
Residue number B
59
Peptide name
Anaphase-promoting complex subunit 11
Ligandability
Cysteine 34 of Anaphase-promoting complex subunit 11
Cysteine 59 of Anaphase-promoting complex subunit 11
5jg6 A 26 A 59
A redox-regulated disulphide may form within Anaphase-promoting complex subunit 11 between cysteines 26 and 59.
Details
Redox score ?
75
PDB code
5jg6
Structure name
apc11-ubv shows role of noncovalent ring-ubiquitin interactions in processive multiubiquitination and ubiquitin chain elongation by apc/c
Structure deposition date
2016-04-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
9
% buried
20
Peptide accession
Q9NYG5
Residue number A
26
Residue number B
59
Peptide name
Anaphase-promoting complex subunit 11
Ligandability
Cysteine 26 of Anaphase-promoting complex subunit 11
Cysteine 59 of Anaphase-promoting complex subunit 11
4r2y B 33 B 37
A redox-regulated disulphide may form within Anaphase-promoting complex subunit 11 between cysteines 33 and 37.
Details
Redox score ?
72
PDB code
4r2y
Structure name
crystal structure of apc11 ring domain
Structure deposition date
2014-08-13
Thiol separation (Å)
5
Half-sphere exposure sum ?
nan
Minimum pKa ?
9
% buried
0
Peptide accession
Q9NYG5
Residue number A
33
Residue number B
37
Peptide name
Anaphase-promoting complex subunit 11
Ligandability
Cysteine 33 of Anaphase-promoting complex subunit 11
Cysteine 37 of Anaphase-promoting complex subunit 11
4r2y D 33 D 34
A redox-regulated disulphide may form within Anaphase-promoting complex subunit 11 between cysteines 33 and 34.
Details
Redox score ?
72
PDB code
4r2y
Structure name
crystal structure of apc11 ring domain
Structure deposition date
2014-08-13
Thiol separation (Å)
7
Half-sphere exposure sum ?
63
Minimum pKa ?
2
% buried
25
Peptide accession
Q9NYG5
Residue number A
33
Residue number B
34
Peptide name
Anaphase-promoting complex subunit 11
Ligandability
Cysteine 33 of Anaphase-promoting complex subunit 11
Cysteine 34 of Anaphase-promoting complex subunit 11
4r2y D 33 D 44
A redox-regulated disulphide may form within Anaphase-promoting complex subunit 11 between cysteines 33 and 44.
Details
Redox score ?
69
PDB code
4r2y
Structure name
crystal structure of apc11 ring domain
Structure deposition date
2014-08-13
Thiol separation (Å)
5
Half-sphere exposure sum ?
50
Minimum pKa ?
9
% buried
12
Peptide accession
Q9NYG5
Residue number A
33
Residue number B
44
Peptide name
Anaphase-promoting complex subunit 11
Ligandability
Cysteine 33 of Anaphase-promoting complex subunit 11
Cysteine 44 of Anaphase-promoting complex subunit 11
4r2y B 26 B 34
A redox-regulated disulphide may form within Anaphase-promoting complex subunit 11 between cysteines 26 and 34.
Details
Redox score ?
68
PDB code
4r2y
Structure name
crystal structure of apc11 ring domain
Structure deposition date
2014-08-13
Thiol separation (Å)
6
Half-sphere exposure sum ?
65
Minimum pKa ?
6
% buried
30
Peptide accession
Q9NYG5
Residue number A
26
Residue number B
34
Peptide name
Anaphase-promoting complex subunit 11
Ligandability
Cysteine 26 of Anaphase-promoting complex subunit 11
Cysteine 34 of Anaphase-promoting complex subunit 11
4r2y C 23 C 44
A redox-regulated disulphide may form within Anaphase-promoting complex subunit 11 between cysteines 23 and 44.
Details
Redox score ?
64
PDB code
4r2y
Structure name
crystal structure of apc11 ring domain
Structure deposition date
2014-08-13
Thiol separation (Å)
8
Half-sphere exposure sum ?
57
Minimum pKa ?
5
% buried
16
Peptide accession
Q9NYG5
Residue number A
23
Residue number B
44
Peptide name
Anaphase-promoting complex subunit 11
Ligandability
Cysteine 23 of Anaphase-promoting complex subunit 11
Cysteine 44 of Anaphase-promoting complex subunit 11
4r2y B 44 B 59
A redox-regulated disulphide may form within Anaphase-promoting complex subunit 11 between cysteines 44 and 59.
Details
Redox score ?
63
PDB code
4r2y
Structure name
crystal structure of apc11 ring domain
Structure deposition date
2014-08-13
Thiol separation (Å)
7
Half-sphere exposure sum ?
57
Minimum pKa ?
8
% buried
30
Peptide accession
Q9NYG5
Residue number A
44
Residue number B
59
Peptide name
Anaphase-promoting complex subunit 11
Ligandability
Cysteine 44 of Anaphase-promoting complex subunit 11
Cysteine 59 of Anaphase-promoting complex subunit 11
4r2y C 23 C 34
A redox-regulated disulphide may form within Anaphase-promoting complex subunit 11 between cysteines 23 and 34.
Details
Redox score ?
63
PDB code
4r2y
Structure name
crystal structure of apc11 ring domain
Structure deposition date
2014-08-13
Thiol separation (Å)
8
Half-sphere exposure sum ?
62
Minimum pKa ?
5
% buried
16
Peptide accession
Q9NYG5
Residue number A
23
Residue number B
34
Peptide name
Anaphase-promoting complex subunit 11
Ligandability
Cysteine 23 of Anaphase-promoting complex subunit 11
Cysteine 34 of Anaphase-promoting complex subunit 11
4r2y C 23 C 54
A redox-regulated disulphide may form within Anaphase-promoting complex subunit 11 between cysteines 23 and 54.
Details
Redox score ?
62
PDB code
4r2y
Structure name
crystal structure of apc11 ring domain
Structure deposition date
2014-08-13
Thiol separation (Å)
7
Half-sphere exposure sum ?
65
Minimum pKa ?
5
% buried
25
Peptide accession
Q9NYG5
Residue number A
23
Residue number B
54
Peptide name
Anaphase-promoting complex subunit 11
Ligandability
Cysteine 23 of Anaphase-promoting complex subunit 11
Cysteine 54 of Anaphase-promoting complex subunit 11
4r2y B 26 B 44
A redox-regulated disulphide may form within Anaphase-promoting complex subunit 11 between cysteines 26 and 44. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
58
PDB code
4r2y
Structure name
crystal structure of apc11 ring domain
Structure deposition date
2014-08-13
Thiol separation (Å)
8
Half-sphere exposure sum ?
55
Minimum pKa ?
8
% buried
20
Peptide accession
Q9NYG5
Residue number A
26
Residue number B
44
Peptide name
Anaphase-promoting complex subunit 11
Ligandability
Cysteine 26 of Anaphase-promoting complex subunit 11
Cysteine 44 of Anaphase-promoting complex subunit 11
2mt5 A 9 A 23
A redox-regulated disulphide may form within Anaphase-promoting complex subunit 11 between cysteines 23 and 37 (9 and 23 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
2mt5
Structure name
isolated ring domain
Structure deposition date
2014-08-13
Thiol separation (Å)
10
Half-sphere exposure sum ?
47
Minimum pKa ?
8
% buried
17
Peptide accession
Q9NYG5
Residue number A
23
Residue number B
37
Peptide name
Anaphase-promoting complex subunit 11
Ligandability
Cysteine 23 of Anaphase-promoting complex subunit 11
Cysteine 37 of Anaphase-promoting complex subunit 11
4r2y A 26 A 33
A redox-regulated disulphide may form within Anaphase-promoting complex subunit 11 between cysteines 26 and 33. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
4r2y
Structure name
crystal structure of apc11 ring domain
Structure deposition date
2014-08-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
54
Minimum pKa ?
9
% buried
6
Peptide accession
Q9NYG5
Residue number A
26
Residue number B
33
Peptide name
Anaphase-promoting complex subunit 11
Ligandability
Cysteine 26 of Anaphase-promoting complex subunit 11
Cysteine 33 of Anaphase-promoting complex subunit 11
2mt5 A 37 A 40
A redox-regulated disulphide may form within Anaphase-promoting complex subunit 11 between cysteines 51 and 54 (37 and 40 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
2mt5
Structure name
isolated ring domain
Structure deposition date
2014-08-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
56
Minimum pKa ?
8
% buried
10
Peptide accession
Q9NYG5
Residue number A
51
Residue number B
54
Peptide name
Anaphase-promoting complex subunit 11
Ligandability
Cysteine 51 of Anaphase-promoting complex subunit 11
Cysteine 54 of Anaphase-promoting complex subunit 11
5jg6 A 23 A 73
A redox-regulated disulphide may form within Anaphase-promoting complex subunit 11 between cysteines 23 and 73. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
5jg6
Structure name
apc11-ubv shows role of noncovalent ring-ubiquitin interactions in processive multiubiquitination and ubiquitin chain elongation by apc/c
Structure deposition date
2016-04-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
60
Minimum pKa ?
6
% buried
34
Peptide accession
Q9NYG5
Residue number A
23
Residue number B
73
Peptide name
Anaphase-promoting complex subunit 11
Ligandability
Cysteine 23 of Anaphase-promoting complex subunit 11
Cysteine 73 of Anaphase-promoting complex subunit 11
5jg6 D 37 D 59
A redox-regulated disulphide may form within Anaphase-promoting complex subunit 11 between cysteines 37 and 59. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
5jg6
Structure name
apc11-ubv shows role of noncovalent ring-ubiquitin interactions in processive multiubiquitination and ubiquitin chain elongation by apc/c
Structure deposition date
2016-04-19
Thiol separation (Å)
8
Half-sphere exposure sum ?
54
Minimum pKa ?
11
% buried
18
Peptide accession
Q9NYG5
Residue number A
37
Residue number B
59
Peptide name
Anaphase-promoting complex subunit 11
Ligandability
Cysteine 37 of Anaphase-promoting complex subunit 11
Cysteine 59 of Anaphase-promoting complex subunit 11
4r2y A 26 A 37
A redox-regulated disulphide may form within Anaphase-promoting complex subunit 11 between cysteines 26 and 37. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
4r2y
Structure name
crystal structure of apc11 ring domain
Structure deposition date
2014-08-13
Thiol separation (Å)
10
Half-sphere exposure sum ?
46
Minimum pKa ?
9
% buried
6
Peptide accession
Q9NYG5
Residue number A
26
Residue number B
37
Peptide name
Anaphase-promoting complex subunit 11
Ligandability
Cysteine 26 of Anaphase-promoting complex subunit 11
Cysteine 37 of Anaphase-promoting complex subunit 11
4r2y A 33 A 59
A redox-regulated disulphide may form within Anaphase-promoting complex subunit 11 between cysteines 33 and 59. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
4r2y
Structure name
crystal structure of apc11 ring domain
Structure deposition date
2014-08-13
Thiol separation (Å)
10
Half-sphere exposure sum ?
59
Minimum pKa ?
9
% buried
16
Peptide accession
Q9NYG5
Residue number A
33
Residue number B
59
Peptide name
Anaphase-promoting complex subunit 11
Ligandability
Cysteine 33 of Anaphase-promoting complex subunit 11
Cysteine 59 of Anaphase-promoting complex subunit 11
2mt5 A 40 A 62
A redox-regulated disulphide may form within Anaphase-promoting complex subunit 11 between cysteines 54 and 76 (40 and 62 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
2mt5
Structure name
isolated ring domain
Structure deposition date
2014-08-13
Thiol separation (Å)
10
Half-sphere exposure sum ?
53
Minimum pKa ?
9
% buried
10
Peptide accession
Q9NYG5
Residue number A
54
Residue number B
76
Peptide name
Anaphase-promoting complex subunit 11
Ligandability
Cysteine 54 of Anaphase-promoting complex subunit 11
Cysteine 76 of Anaphase-promoting complex subunit 11
5lcw B 54 B 73
A redox-regulated disulphide may form within Anaphase-promoting complex subunit 11 between cysteines 54 and 73. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
5lcw
Structure name
cryo-em structure of the anaphase-promoting complex/cyclosome, in complex with the mitotic checkpoint complex (apc/c-mcc) at 4
Structure deposition date
2016-06-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
65
Minimum pKa ?
9
% buried
22
Peptide accession
Q9NYG5
Residue number A
54
Residue number B
73
Peptide name
Anaphase-promoting complex subunit 11
Ligandability
Cysteine 54 of Anaphase-promoting complex subunit 11
Cysteine 73 of Anaphase-promoting complex subunit 11
6tlj B 26 B 54
A redox-regulated disulphide may form within Anaphase-promoting complex subunit 11 between cysteines 26 and 54. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
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)
10
Half-sphere exposure sum ?
63
Minimum pKa ?
10
% buried
nan
Peptide accession
Q9NYG5
Residue number A
26
Residue number B
54
Peptide name
Anaphase-promoting complex subunit 11
Ligandability
Cysteine 26 of Anaphase-promoting complex subunit 11
Cysteine 54 of Anaphase-promoting complex subunit 11
5g04 B 44 B 54
A redox-regulated disulphide may form within Anaphase-promoting complex subunit 11 between cysteines 44 and 54. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
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 ?
67
Minimum pKa ?
10
% buried
48
Peptide accession
Q9NYG5
Residue number A
44
Residue number B
54
Peptide name
Anaphase-promoting complex subunit 11
Ligandability
Cysteine 44 of Anaphase-promoting complex subunit 11
Cysteine 54 of Anaphase-promoting complex subunit 11
6tnt B 54 B 59
A redox-regulated disulphide may form within Anaphase-promoting complex subunit 11 between cysteines 54 and 59. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
31
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 ?
68
Minimum pKa ?
12
% buried
52
Peptide accession
Q9NYG5
Residue number A
54
Residue number B
59
Peptide name
Anaphase-promoting complex subunit 11
Ligandability
Cysteine 54 of Anaphase-promoting complex subunit 11
Cysteine 59 of Anaphase-promoting complex subunit 11
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