Cell division cycle protein 27 homolog
Intramolecular
Cysteine 66 and cysteine 71
Cysteine 673 and cysteine 705
Cysteine 156 and cysteine 477
Cysteine 78 and cysteine 79
Cysteine 66 and cysteine 78
Cysteine 126 and cysteine 137
Cysteine 66 and cysteine 79
Cysteine 477 and cysteine 481
Cysteine 71 and cysteine 78
Cysteine 115 and cysteine 137
4rg6 A 66 A 71
A redox-regulated disulphide may form within Cell division cycle protein 27 homolog between cysteines 66 and 71.
Details
Redox score ?
82
PDB code
4rg6
Structure name
crystal structure of apc3-apc16 complex
Structure deposition date
2014-09-29
Thiol separation (Å)
3
Half-sphere exposure sum ?
60
Minimum pKa ?
9
% buried
40
Peptide accession
P30260
Residue number A
66
Residue number B
71
Peptide name
Cell division cycle protein 27 homolog
Ligandability
Cysteine 66 of Cell division cycle protein 27 homolog
Cysteine 71 of Cell division cycle protein 27 homolog
6tnt H 673 H 705
A redox-regulated disulphide may form within Cell division cycle protein 27 homolog between cysteines 673 and 705.
Details
Redox score ?
71
PDB code
6tnt
Structure name
sumoylated apoapc/c with repositioned apc2 whb domain
Structure deposition date
2019-12-10
Thiol separation (Å)
3
Half-sphere exposure sum ?
86
Minimum pKa ?
9
% buried
90
Peptide accession
P30260
Residue number A
673
Residue number B
705
Peptide name
Cell division cycle protein 27 homolog
Ligandability
Cysteine 673 of Cell division cycle protein 27 homolog
Cysteine 705 of Cell division cycle protein 27 homolog
4rg6 B 156 B 483
A redox-regulated disulphide may form within Cell division cycle protein 27 homolog between cysteines 156 and 477 (156 and 483 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
56
PDB code
4rg6
Structure name
crystal structure of apc3-apc16 complex
Structure deposition date
2014-09-29
Thiol separation (Å)
5
Half-sphere exposure sum ?
64
Minimum pKa ?
12
% buried
86
Peptide accession
P30260
Residue number A
156
Residue number B
477
Peptide name
Cell division cycle protein 27 homolog
Ligandability
Cysteine 156 of Cell division cycle protein 27 homolog
Cysteine 477 of Cell division cycle protein 27 homolog
4rg9 B 78 B 79
A redox-regulated disulphide may form within Cell division cycle protein 27 homolog between cysteines 78 and 79. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
4rg9
Structure name
crystal structure of apc3-apc16 complex (selenomethionine derivative)
Structure deposition date
2014-09-29
Thiol separation (Å)
7
Half-sphere exposure sum ?
69
Minimum pKa ?
12
% buried
71
Peptide accession
P30260
Residue number A
78
Residue number B
79
Peptide name
Cell division cycle protein 27 homolog
Ligandability
Cysteine 78 of Cell division cycle protein 27 homolog
Cysteine 79 of Cell division cycle protein 27 homolog
4rg9 B 66 B 78
A redox-regulated disulphide may form within Cell division cycle protein 27 homolog between cysteines 66 and 78. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
4rg9
Structure name
crystal structure of apc3-apc16 complex (selenomethionine derivative)
Structure deposition date
2014-09-29
Thiol separation (Å)
10
Half-sphere exposure sum ?
65
Minimum pKa ?
7
% buried
71
Peptide accession
P30260
Residue number A
66
Residue number B
78
Peptide name
Cell division cycle protein 27 homolog
Ligandability
Cysteine 66 of Cell division cycle protein 27 homolog
Cysteine 78 of Cell division cycle protein 27 homolog
4rg9 A 126 A 137
A redox-regulated disulphide may form within Cell division cycle protein 27 homolog between cysteines 126 and 137. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
4rg9
Structure name
crystal structure of apc3-apc16 complex (selenomethionine derivative)
Structure deposition date
2014-09-29
Thiol separation (Å)
8
Half-sphere exposure sum ?
68
Minimum pKa ?
10
% buried
64
Peptide accession
P30260
Residue number A
126
Residue number B
137
Peptide name
Cell division cycle protein 27 homolog
Ligandability
Cysteine 126 of Cell division cycle protein 27 homolog
Cysteine 137 of Cell division cycle protein 27 homolog
4rg6 B 66 B 79
A redox-regulated disulphide may form within Cell division cycle protein 27 homolog between cysteines 66 and 79. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
4rg6
Structure name
crystal structure of apc3-apc16 complex
Structure deposition date
2014-09-29
Thiol separation (Å)
9
Half-sphere exposure sum ?
59
Minimum pKa ?
11
% buried
54
Peptide accession
P30260
Residue number A
66
Residue number B
79
Peptide name
Cell division cycle protein 27 homolog
Ligandability
Cysteine 66 of Cell division cycle protein 27 homolog
Cysteine 79 of Cell division cycle protein 27 homolog
4rg9 B 483 B 487
A redox-regulated disulphide may form within Cell division cycle protein 27 homolog between cysteines 477 and 481 (483 and 487 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
30
PDB code
4rg9
Structure name
crystal structure of apc3-apc16 complex (selenomethionine derivative)
Structure deposition date
2014-09-29
Thiol separation (Å)
10
Half-sphere exposure sum ?
66
Minimum pKa ?
12
% buried
88
Peptide accession
P30260
Residue number A
477
Residue number B
481
Peptide name
Cell division cycle protein 27 homolog
Ligandability
Cysteine 477 of Cell division cycle protein 27 homolog
Cysteine 481 of Cell division cycle protein 27 homolog
6q6h P 71 P 78
A redox-regulated disulphide may form within Cell division cycle protein 27 homolog between cysteines 71 and 78. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
28
PDB code
6q6h
Structure name
cryo-em structure of the apc/c-cdc20-cdk2-cyclina2-cks2 complex, the d2 box class
Structure deposition date
2018-12-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
75
Minimum pKa ?
13
% buried
75
Peptide accession
P30260
Residue number A
71
Residue number B
78
Peptide name
Cell division cycle protein 27 homolog
Ligandability
Cysteine 71 of Cell division cycle protein 27 homolog
Cysteine 78 of Cell division cycle protein 27 homolog
6tm5 H 115 H 137
A redox-regulated disulphide may form within Cell division cycle protein 27 homolog 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 ?
25
PDB code
6tm5
Structure name
cryo-em structure of the anaphase-promoting complex/cyclosome, in complex with the nek2a substrate at 3
Structure deposition date
2019-12-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
78
Minimum pKa ?
12
% buried
96
Peptide accession
P30260
Residue number A
115
Residue number B
137
Peptide name
Cell division cycle protein 27 homolog
Ligandability
Cysteine 115 of Cell division cycle protein 27 homolog
Cysteine 137 of Cell division cycle protein 27 homolog
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