Apoptotic protease-activating factor 1
Intermolecular
Cysteine 258 and cysteine 115 L
Intramolecular
Cysteine 633 and cysteine 663
Cysteine 803 and cysteine 846 L
Cysteine 704 and cysteine 749
Cysteine 675 and cysteine 705 L
Cysteine 761 and cysteine 804
Cysteine 662 and cysteine 705
Cysteine 662 and cysteine 675 L
Cysteine 804 and cysteine 846
Cysteine 705 and cysteine 749
More...Cysteine 803 and cysteine 804 L
Cysteine 622 and cysteine 663
Cysteine 704 and cysteine 705
Cysteine 749 and cysteine 804
Cysteine 538 and cysteine 541
Cysteine 501 and cysteine 541
Cysteine 966 and cysteine 967
Cysteine 704 and cysteine 804
Cysteine 662 and cysteine 704
Cysteine 662 and cysteine 749
Cysteine 662 and cysteine 663
Cysteine 1083 and cysteine 1091
Cysteine 426 and cysteine 434
Cysteine 663 and cysteine 675 L
Cysteine 622 and cysteine 633
Cysteine 675 and cysteine 749 L
Cysteine 501 and cysteine 538
Cysteine 633 and cysteine 662
Cysteine 761 and cysteine 803 L
Cysteine 749 and cysteine 761
Cysteine 675 and cysteine 704 L
Cysteine 633 and cysteine 675 L
Cysteine 878 and cysteine 915
Cysteine 761 and cysteine 846
Cysteine 633 and cysteine 705
Cysteine 967 and cysteine 968
Cysteine 663 and cysteine 705
Cysteine 966 and cysteine 968
Cysteine 704 and cysteine 761
Cysteine 622 and cysteine 705
5wve K 258 M 115
A redox-regulated disulphide may form between two units of Apoptotic protease-activating factor 1 at cysteines 258 and 115. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
35
PDB code
5wve
Structure name
apaf-1-caspase-9 holoenzyme
Structure deposition date
2016-12-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
75
Minimum pKa ?
11
% buried
86
Peptide A name
Apoptotic protease-activating factor 1
Peptide B name
Apoptotic protease-activating factor 1
Peptide A accession
O14727
Peptide B accession
O14727
Peptide A residue number
258
Peptide B residue number
115
Ligandability
Cysteine 258 of Apoptotic protease-activating factor 1
Cysteine 115 of Apoptotic protease-activating factor 1
3j2t D 633 D 663
A redox-regulated disulphide may form within Apoptotic protease-activating factor 1 between cysteines 633 and 663.
Details
Redox score ?
82
PDB code
3j2t
Structure name
an improved model of the human apoptosome
Structure deposition date
2012-12-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
86
Minimum pKa ?
nan
% buried
nan
Peptide accession
O14727
Residue number A
633
Residue number B
663
Peptide name
Apoptotic protease-activating factor 1
Ligandability
Cysteine 633 of Apoptotic protease-activating factor 1
Cysteine 663 of Apoptotic protease-activating factor 1
3j2t G 803 G 846
A redox-regulated disulphide may form within Apoptotic protease-activating factor 1 between cysteines 803 and 846.
Details
Redox score ?
80
PDB code
3j2t
Structure name
an improved model of the human apoptosome
Structure deposition date
2012-12-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
O14727
Residue number A
803
Residue number B
846
Peptide name
Apoptotic protease-activating factor 1
Ligandability
Cysteine 803 of Apoptotic protease-activating factor 1
Cysteine 846 of Apoptotic protease-activating factor 1
3j2t E 704 E 749
A redox-regulated disulphide may form within Apoptotic protease-activating factor 1 between cysteines 704 and 749.
Details
Redox score ?
80
PDB code
3j2t
Structure name
an improved model of the human apoptosome
Structure deposition date
2012-12-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
85
Minimum pKa ?
nan
% buried
nan
Peptide accession
O14727
Residue number A
704
Residue number B
749
Peptide name
Apoptotic protease-activating factor 1
Ligandability
Cysteine 704 of Apoptotic protease-activating factor 1
Cysteine 749 of Apoptotic protease-activating factor 1
3j2t E 675 E 705
A redox-regulated disulphide may form within Apoptotic protease-activating factor 1 between cysteines 675 and 705.
Details
Redox score ?
79
PDB code
3j2t
Structure name
an improved model of the human apoptosome
Structure deposition date
2012-12-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
92
Minimum pKa ?
nan
% buried
nan
Peptide accession
O14727
Residue number A
675
Residue number B
705
Peptide name
Apoptotic protease-activating factor 1
Ligandability
Cysteine 675 of Apoptotic protease-activating factor 1
Cysteine 705 of Apoptotic protease-activating factor 1
5wve I 761 I 804
A redox-regulated disulphide may form within Apoptotic protease-activating factor 1 between cysteines 761 and 804.
Details
Redox score ?
79
PDB code
5wve
Structure name
apaf-1-caspase-9 holoenzyme
Structure deposition date
2016-12-24
Thiol separation (Å)
2
Half-sphere exposure sum ?
89
Minimum pKa ?
nan
% buried
nan
Peptide accession
O14727
Residue number A
761
Residue number B
804
Peptide name
Apoptotic protease-activating factor 1
Ligandability
Cysteine 761 of Apoptotic protease-activating factor 1
Cysteine 804 of Apoptotic protease-activating factor 1
5juy F 662 F 705
A redox-regulated disulphide may form within Apoptotic protease-activating factor 1 between cysteines 662 and 705.
Details
Redox score ?
65
PDB code
5juy
Structure name
active human apoptosome with procaspase-9
Structure deposition date
2016-05-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
78
Minimum pKa ?
12
% buried
nan
Peptide accession
O14727
Residue number A
662
Residue number B
705
Peptide name
Apoptotic protease-activating factor 1
Ligandability
Cysteine 662 of Apoptotic protease-activating factor 1
Cysteine 705 of Apoptotic protease-activating factor 1
5wve M 662 M 675
A redox-regulated disulphide may form within Apoptotic protease-activating factor 1 between cysteines 662 and 675.
Details
Redox score ?
61
PDB code
5wve
Structure name
apaf-1-caspase-9 holoenzyme
Structure deposition date
2016-12-24
Thiol separation (Å)
3
Half-sphere exposure sum ?
91
Minimum pKa ?
12
% buried
nan
Peptide accession
O14727
Residue number A
662
Residue number B
675
Peptide name
Apoptotic protease-activating factor 1
Ligandability
Cysteine 662 of Apoptotic protease-activating factor 1
Cysteine 675 of Apoptotic protease-activating factor 1
5juy F 804 F 846
A redox-regulated disulphide may form within Apoptotic protease-activating factor 1 between cysteines 804 and 846. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
53
PDB code
5juy
Structure name
active human apoptosome with procaspase-9
Structure deposition date
2016-05-10
Thiol separation (Å)
7
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
O14727
Residue number A
804
Residue number B
846
Peptide name
Apoptotic protease-activating factor 1
Ligandability
Cysteine 804 of Apoptotic protease-activating factor 1
Cysteine 846 of Apoptotic protease-activating factor 1
5juy C 705 C 749
A redox-regulated disulphide may form within Apoptotic protease-activating factor 1 between cysteines 705 and 749. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
5juy
Structure name
active human apoptosome with procaspase-9
Structure deposition date
2016-05-10
Thiol separation (Å)
7
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
O14727
Residue number A
705
Residue number B
749
Peptide name
Apoptotic protease-activating factor 1
Ligandability
Cysteine 705 of Apoptotic protease-activating factor 1
Cysteine 749 of Apoptotic protease-activating factor 1
3shf A 803 A 804
A redox-regulated disulphide may form within Apoptotic protease-activating factor 1 between cysteines 803 and 804. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
3shf
Structure name
crystal structure of the r265s mutant of full-length murine apaf-1
Structure deposition date
2011-06-16
Thiol separation (Å)
7
Half-sphere exposure sum ?
90
Minimum pKa ?
nan
% buried
nan
Peptide accession
A2RRK8
Residue number A
803
Residue number B
804
Peptide name
Apoptotic protease-activating factor 1
Ligandability
Cysteine 803 of Apoptotic protease-activating factor 1
Cysteine 804 of Apoptotic protease-activating factor 1
5juy B 622 B 663
A redox-regulated disulphide may form within Apoptotic protease-activating factor 1 between cysteines 622 and 663. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
5juy
Structure name
active human apoptosome with procaspase-9
Structure deposition date
2016-05-10
Thiol separation (Å)
6
Half-sphere exposure sum ?
80
Minimum pKa ?
12
% buried
nan
Peptide accession
O14727
Residue number A
622
Residue number B
663
Peptide name
Apoptotic protease-activating factor 1
Ligandability
Cysteine 622 of Apoptotic protease-activating factor 1
Cysteine 663 of Apoptotic protease-activating factor 1
3jbt I 704 I 705
A redox-regulated disulphide may form within Apoptotic protease-activating factor 1 between cysteines 704 and 705. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
3jbt
Structure name
atomic structure of the apaf-1 apoptosome
Structure deposition date
2015-10-15
Thiol separation (Å)
7
Half-sphere exposure sum ?
92
Minimum pKa ?
nan
% buried
nan
Peptide accession
O14727
Residue number A
704
Residue number B
705
Peptide name
Apoptotic protease-activating factor 1
Ligandability
Cysteine 704 of Apoptotic protease-activating factor 1
Cysteine 705 of Apoptotic protease-activating factor 1
3sfz A 749 A 804
A redox-regulated disulphide may form within Apoptotic protease-activating factor 1 between cysteines 749 and 804. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
3sfz
Structure name
crystal structure of full-length murine apaf-1
Structure deposition date
2011-06-14
Thiol separation (Å)
8
Half-sphere exposure sum ?
90
Minimum pKa ?
nan
% buried
nan
Peptide accession
A2RRK8
Residue number A
749
Residue number B
804
Peptide name
Apoptotic protease-activating factor 1
Ligandability
Cysteine 749 of Apoptotic protease-activating factor 1
Cysteine 804 of Apoptotic protease-activating factor 1
3sfz A 538 A 541
A redox-regulated disulphide may form within Apoptotic protease-activating factor 1 between cysteines 538 and 541. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
3sfz
Structure name
crystal structure of full-length murine apaf-1
Structure deposition date
2011-06-14
Thiol separation (Å)
8
Half-sphere exposure sum ?
52
Minimum pKa ?
10
% buried
40
Peptide accession
A2RRK8
Residue number A
538
Residue number B
541
Peptide name
Apoptotic protease-activating factor 1
Ligandability
Cysteine 538 of Apoptotic protease-activating factor 1
Cysteine 541 of Apoptotic protease-activating factor 1
3shf A 501 A 541
A redox-regulated disulphide may form within Apoptotic protease-activating factor 1 between cysteines 501 and 541. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
3shf
Structure name
crystal structure of the r265s mutant of full-length murine apaf-1
Structure deposition date
2011-06-16
Thiol separation (Å)
8
Half-sphere exposure sum ?
65
Minimum pKa ?
10
% buried
58
Peptide accession
A2RRK8
Residue number A
501
Residue number B
541
Peptide name
Apoptotic protease-activating factor 1
Ligandability
Cysteine 501 of Apoptotic protease-activating factor 1
Cysteine 541 of Apoptotic protease-activating factor 1
5wve E 966 E 967
A redox-regulated disulphide may form within Apoptotic protease-activating factor 1 between cysteines 966 and 967. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
5wve
Structure name
apaf-1-caspase-9 holoenzyme
Structure deposition date
2016-12-24
Thiol separation (Å)
7
Half-sphere exposure sum ?
78
Minimum pKa ?
11
% buried
84
Peptide accession
O14727
Residue number A
966
Residue number B
967
Peptide name
Apoptotic protease-activating factor 1
Ligandability
Cysteine 966 of Apoptotic protease-activating factor 1
Cysteine 967 of Apoptotic protease-activating factor 1
3sfz A 704 A 804
A redox-regulated disulphide may form within Apoptotic protease-activating factor 1 between cysteines 704 and 804. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
3sfz
Structure name
crystal structure of full-length murine apaf-1
Structure deposition date
2011-06-14
Thiol separation (Å)
7
Half-sphere exposure sum ?
95
Minimum pKa ?
nan
% buried
nan
Peptide accession
A2RRK8
Residue number A
704
Residue number B
804
Peptide name
Apoptotic protease-activating factor 1
Ligandability
Cysteine 704 of Apoptotic protease-activating factor 1
Cysteine 804 of Apoptotic protease-activating factor 1
5wve E 662 E 704
A redox-regulated disulphide may form within Apoptotic protease-activating factor 1 between cysteines 662 and 704. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
5wve
Structure name
apaf-1-caspase-9 holoenzyme
Structure deposition date
2016-12-24
Thiol separation (Å)
6
Half-sphere exposure sum ?
89
Minimum pKa ?
12
% buried
nan
Peptide accession
O14727
Residue number A
662
Residue number B
704
Peptide name
Apoptotic protease-activating factor 1
Ligandability
Cysteine 662 of Apoptotic protease-activating factor 1
Cysteine 704 of Apoptotic protease-activating factor 1
5juy D 662 D 749
A redox-regulated disulphide may form within Apoptotic protease-activating factor 1 between cysteines 662 and 749. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
5juy
Structure name
active human apoptosome with procaspase-9
Structure deposition date
2016-05-10
Thiol separation (Å)
7
Half-sphere exposure sum ?
80
Minimum pKa ?
12
% buried
nan
Peptide accession
O14727
Residue number A
662
Residue number B
749
Peptide name
Apoptotic protease-activating factor 1
Ligandability
Cysteine 662 of Apoptotic protease-activating factor 1
Cysteine 749 of Apoptotic protease-activating factor 1
5juy B 662 B 663
A redox-regulated disulphide may form within Apoptotic protease-activating factor 1 between cysteines 662 and 663. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
5juy
Structure name
active human apoptosome with procaspase-9
Structure deposition date
2016-05-10
Thiol separation (Å)
7
Half-sphere exposure sum ?
81
Minimum pKa ?
12
% buried
nan
Peptide accession
O14727
Residue number A
662
Residue number B
663
Peptide name
Apoptotic protease-activating factor 1
Ligandability
Cysteine 662 of Apoptotic protease-activating factor 1
Cysteine 663 of Apoptotic protease-activating factor 1
5wve G 1083 G 1091
A redox-regulated disulphide may form within Apoptotic protease-activating factor 1 between cysteines 1083 and 1091. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
5wve
Structure name
apaf-1-caspase-9 holoenzyme
Structure deposition date
2016-12-24
Thiol separation (Å)
7
Half-sphere exposure sum ?
83
Minimum pKa ?
12
% buried
93
Peptide accession
O14727
Residue number A
1083
Residue number B
1091
Peptide name
Apoptotic protease-activating factor 1
Ligandability
Cysteine 1083 of Apoptotic protease-activating factor 1
Cysteine 1091 of Apoptotic protease-activating factor 1
3shf A 426 A 434
A redox-regulated disulphide may form within Apoptotic protease-activating factor 1 between cysteines 426 and 434. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
3shf
Structure name
crystal structure of the r265s mutant of full-length murine apaf-1
Structure deposition date
2011-06-16
Thiol separation (Å)
8
Half-sphere exposure sum ?
68
Minimum pKa ?
11
% buried
71
Peptide accession
A2RRK8
Residue number A
426
Residue number B
434
Peptide name
Apoptotic protease-activating factor 1
Ligandability
Cysteine 426 of Apoptotic protease-activating factor 1
Cysteine 434 of Apoptotic protease-activating factor 1
5wve C 663 C 675
A redox-regulated disulphide may form within Apoptotic protease-activating factor 1 between cysteines 663 and 675. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
5wve
Structure name
apaf-1-caspase-9 holoenzyme
Structure deposition date
2016-12-24
Thiol separation (Å)
8
Half-sphere exposure sum ?
93
Minimum pKa ?
nan
% buried
nan
Peptide accession
O14727
Residue number A
663
Residue number B
675
Peptide name
Apoptotic protease-activating factor 1
Ligandability
Cysteine 663 of Apoptotic protease-activating factor 1
Cysteine 675 of Apoptotic protease-activating factor 1
5wve K 622 K 633
A redox-regulated disulphide may form within Apoptotic protease-activating factor 1 between cysteines 622 and 633. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
5wve
Structure name
apaf-1-caspase-9 holoenzyme
Structure deposition date
2016-12-24
Thiol separation (Å)
7
Half-sphere exposure sum ?
88
Minimum pKa ?
12
% buried
nan
Peptide accession
O14727
Residue number A
622
Residue number B
633
Peptide name
Apoptotic protease-activating factor 1
Ligandability
Cysteine 622 of Apoptotic protease-activating factor 1
Cysteine 633 of Apoptotic protease-activating factor 1
5juy E 675 E 749
A redox-regulated disulphide may form within Apoptotic protease-activating factor 1 between cysteines 675 and 749. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
5juy
Structure name
active human apoptosome with procaspase-9
Structure deposition date
2016-05-10
Thiol separation (Å)
9
Half-sphere exposure sum ?
85
Minimum pKa ?
nan
% buried
nan
Peptide accession
O14727
Residue number A
675
Residue number B
749
Peptide name
Apoptotic protease-activating factor 1
Ligandability
Cysteine 675 of Apoptotic protease-activating factor 1
Cysteine 749 of Apoptotic protease-activating factor 1
3j2t C 501 C 538
A redox-regulated disulphide may form within Apoptotic protease-activating factor 1 between cysteines 501 and 538. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
3j2t
Structure name
an improved model of the human apoptosome
Structure deposition date
2012-12-23
Thiol separation (Å)
10
Half-sphere exposure sum ?
57
Minimum pKa ?
10
% buried
21
Peptide accession
O14727
Residue number A
501
Residue number B
538
Peptide name
Apoptotic protease-activating factor 1
Ligandability
Cysteine 501 of Apoptotic protease-activating factor 1
Cysteine 538 of Apoptotic protease-activating factor 1
5juy A 633 A 662
A redox-regulated disulphide may form within Apoptotic protease-activating factor 1 between cysteines 633 and 662. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
5juy
Structure name
active human apoptosome with procaspase-9
Structure deposition date
2016-05-10
Thiol separation (Å)
7
Half-sphere exposure sum ?
83
Minimum pKa ?
12
% buried
nan
Peptide accession
O14727
Residue number A
633
Residue number B
662
Peptide name
Apoptotic protease-activating factor 1
Ligandability
Cysteine 633 of Apoptotic protease-activating factor 1
Cysteine 662 of Apoptotic protease-activating factor 1
5juy E 761 E 803
A redox-regulated disulphide may form within Apoptotic protease-activating factor 1 between cysteines 761 and 803. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
5juy
Structure name
active human apoptosome with procaspase-9
Structure deposition date
2016-05-10
Thiol separation (Å)
9
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
O14727
Residue number A
761
Residue number B
803
Peptide name
Apoptotic protease-activating factor 1
Ligandability
Cysteine 761 of Apoptotic protease-activating factor 1
Cysteine 803 of Apoptotic protease-activating factor 1
5juy A 749 A 761
A redox-regulated disulphide may form within Apoptotic protease-activating factor 1 between cysteines 749 and 761. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
5juy
Structure name
active human apoptosome with procaspase-9
Structure deposition date
2016-05-10
Thiol separation (Å)
9
Half-sphere exposure sum ?
86
Minimum pKa ?
nan
% buried
nan
Peptide accession
O14727
Residue number A
749
Residue number B
761
Peptide name
Apoptotic protease-activating factor 1
Ligandability
Cysteine 749 of Apoptotic protease-activating factor 1
Cysteine 761 of Apoptotic protease-activating factor 1
3j2t E 675 E 704
A redox-regulated disulphide may form within Apoptotic protease-activating factor 1 between cysteines 675 and 704. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
3j2t
Structure name
an improved model of the human apoptosome
Structure deposition date
2012-12-23
Thiol separation (Å)
8
Half-sphere exposure sum ?
93
Minimum pKa ?
nan
% buried
nan
Peptide accession
O14727
Residue number A
675
Residue number B
704
Peptide name
Apoptotic protease-activating factor 1
Ligandability
Cysteine 675 of Apoptotic protease-activating factor 1
Cysteine 704 of Apoptotic protease-activating factor 1
5wve E 633 E 675
A redox-regulated disulphide may form within Apoptotic protease-activating factor 1 between cysteines 633 and 675. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
5wve
Structure name
apaf-1-caspase-9 holoenzyme
Structure deposition date
2016-12-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
92
Minimum pKa ?
nan
% buried
nan
Peptide accession
O14727
Residue number A
633
Residue number B
675
Peptide name
Apoptotic protease-activating factor 1
Ligandability
Cysteine 633 of Apoptotic protease-activating factor 1
Cysteine 675 of Apoptotic protease-activating factor 1
5juy G 878 G 915
A redox-regulated disulphide may form within Apoptotic protease-activating factor 1 between cysteines 878 and 915. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
5juy
Structure name
active human apoptosome with procaspase-9
Structure deposition date
2016-05-10
Thiol separation (Å)
10
Half-sphere exposure sum ?
69
Minimum pKa ?
9
% buried
50
Peptide accession
O14727
Residue number A
878
Residue number B
915
Peptide name
Apoptotic protease-activating factor 1
Ligandability
Cysteine 878 of Apoptotic protease-activating factor 1
Cysteine 915 of Apoptotic protease-activating factor 1
5juy B 761 B 846
A redox-regulated disulphide may form within Apoptotic protease-activating factor 1 between cysteines 761 and 846. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
5juy
Structure name
active human apoptosome with procaspase-9
Structure deposition date
2016-05-10
Thiol separation (Å)
9
Half-sphere exposure sum ?
87
Minimum pKa ?
nan
% buried
nan
Peptide accession
O14727
Residue number A
761
Residue number B
846
Peptide name
Apoptotic protease-activating factor 1
Ligandability
Cysteine 761 of Apoptotic protease-activating factor 1
Cysteine 846 of Apoptotic protease-activating factor 1
5juy D 633 D 705
A redox-regulated disulphide may form within Apoptotic protease-activating factor 1 between cysteines 633 and 705. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
5juy
Structure name
active human apoptosome with procaspase-9
Structure deposition date
2016-05-10
Thiol separation (Å)
9
Half-sphere exposure sum ?
83
Minimum pKa ?
nan
% buried
nan
Peptide accession
O14727
Residue number A
633
Residue number B
705
Peptide name
Apoptotic protease-activating factor 1
Ligandability
Cysteine 633 of Apoptotic protease-activating factor 1
Cysteine 705 of Apoptotic protease-activating factor 1
3shf A 967 A 968
A redox-regulated disulphide may form within Apoptotic protease-activating factor 1 between cysteines 967 and 968. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
3shf
Structure name
crystal structure of the r265s mutant of full-length murine apaf-1
Structure deposition date
2011-06-16
Thiol separation (Å)
7
Half-sphere exposure sum ?
87
Minimum pKa ?
13
% buried
100
Peptide accession
A2RRK8
Residue number A
967
Residue number B
968
Peptide name
Apoptotic protease-activating factor 1
Ligandability
Cysteine 967 of Apoptotic protease-activating factor 1
Cysteine 968 of Apoptotic protease-activating factor 1
3j2t C 663 C 705
A redox-regulated disulphide may form within Apoptotic protease-activating factor 1 between cysteines 663 and 705. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
36
PDB code
3j2t
Structure name
an improved model of the human apoptosome
Structure deposition date
2012-12-23
Thiol separation (Å)
10
Half-sphere exposure sum ?
89
Minimum pKa ?
nan
% buried
nan
Peptide accession
O14727
Residue number A
663
Residue number B
705
Peptide name
Apoptotic protease-activating factor 1
Ligandability
Cysteine 663 of Apoptotic protease-activating factor 1
Cysteine 705 of Apoptotic protease-activating factor 1
3shf A 966 A 968
A redox-regulated disulphide may form within Apoptotic protease-activating factor 1 between cysteines 966 and 968. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
35
PDB code
3shf
Structure name
crystal structure of the r265s mutant of full-length murine apaf-1
Structure deposition date
2011-06-16
Thiol separation (Å)
7
Half-sphere exposure sum ?
86
Minimum pKa ?
12
% buried
100
Peptide accession
A2RRK8
Residue number A
966
Residue number B
968
Peptide name
Apoptotic protease-activating factor 1
Ligandability
Cysteine 966 of Apoptotic protease-activating factor 1
Cysteine 968 of Apoptotic protease-activating factor 1
3j2t A 704 A 761
A redox-regulated disulphide may form within Apoptotic protease-activating factor 1 between cysteines 704 and 761. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
3j2t
Structure name
an improved model of the human apoptosome
Structure deposition date
2012-12-23
Thiol separation (Å)
9
Half-sphere exposure sum ?
93
Minimum pKa ?
nan
% buried
nan
Peptide accession
O14727
Residue number A
704
Residue number B
761
Peptide name
Apoptotic protease-activating factor 1
Ligandability
Cysteine 704 of Apoptotic protease-activating factor 1
Cysteine 761 of Apoptotic protease-activating factor 1
3shf A 622 A 705
A redox-regulated disulphide may form within Apoptotic protease-activating factor 1 between cysteines 622 and 705. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
32
PDB code
3shf
Structure name
crystal structure of the r265s mutant of full-length murine apaf-1
Structure deposition date
2011-06-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
91
Minimum pKa ?
12
% buried
nan
Peptide accession
A2RRK8
Residue number A
622
Residue number B
705
Peptide name
Apoptotic protease-activating factor 1
Ligandability
Cysteine 622 of Apoptotic protease-activating factor 1
Cysteine 705 of Apoptotic protease-activating factor 1
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