Caspase-9
Intermolecular
Cysteine 287 and cysteine 188 of Effector protein NleF
Cysteine 403 and cysteine 403
Intramolecular
Cysteine 160 and cysteine 229
Cysteine 230 and cysteine 272
Cysteine 172 and cysteine 256
Cysteine 239 and cysteine 256
Cysteine 229 and cysteine 230
Cysteine 163 and cysteine 230
Cysteine 163 and cysteine 187
Cysteine 163 and cysteine 229
More...Cysteine 239 and cysteine 287
Cysteine 160 and cysteine 230
3v3k M 285 N 188
A redox-regulated disulphide may form between cysteine 287 of Caspase-9 and cysteine 188 of Effector protein NleF (285 and 188 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
52
PDB code
3v3k
Structure name
human caspase 9 in complex with bacterial effector protein
Structure deposition date
2011-12-13
Thiol separation (Å)
5
Half-sphere exposure sum ?
90
Minimum pKa ?
11
% buried
100
Peptide A name
Caspase-9
Peptide B name
Effector protein NleF
Peptide A accession
P55211
Peptide B accession
Q8XAL7
Peptide A residue number
287
Peptide B residue number
188
Ligandability
Cysteine 287 of Caspase-9
Cysteine 188 of Effector protein NleF
3v3k M 389 O 389
A redox-regulated disulphide may form between two units of Caspase-9 at cysteines 403 and 403 (389 and 389 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
27
PDB code
3v3k
Structure name
human caspase 9 in complex with bacterial effector protein
Structure deposition date
2011-12-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
86
Minimum pKa ?
12
% buried
100
Peptide A name
Caspase-9
Peptide B name
Caspase-9
Peptide A accession
P55211
Peptide B accession
P55211
Peptide A residue number
403
Peptide B residue number
403
Ligandability
1nw9 B 160 B 229
A redox-regulated disulphide may form within Caspase-9 between cysteines 160 and 229. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
54
PDB code
1nw9
Structure name
structure of caspase-9 in an inhibitory complex with xiap-bir3
Structure deposition date
2003-02-05
Thiol separation (Å)
5
Half-sphere exposure sum ?
79
Minimum pKa ?
12
% buried
89
Peptide accession
P55211
Residue number A
160
Residue number B
229
Peptide name
Caspase-9
Ligandability
Cysteine 160 of Caspase-9
Cysteine 229 of Caspase-9
3v3k O 230 O 270
A redox-regulated disulphide may form within Caspase-9 between cysteines 230 and 272 (230 and 270 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
3v3k
Structure name
human caspase 9 in complex with bacterial effector protein
Structure deposition date
2011-12-13
Thiol separation (Å)
7
Half-sphere exposure sum ?
75
Minimum pKa ?
10
% buried
74
Peptide accession
P55211
Residue number A
230
Residue number B
272
Peptide name
Caspase-9
Ligandability
Cysteine 230 of Caspase-9
Cysteine 272 of Caspase-9
3v3k G 174 G 254
A redox-regulated disulphide may form within Caspase-9 between cysteines 172 and 256 (174 and 254 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
3v3k
Structure name
human caspase 9 in complex with bacterial effector protein
Structure deposition date
2011-12-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
49
Minimum pKa ?
8
% buried
14
Peptide accession
P55211
Residue number A
172
Residue number B
256
Peptide name
Caspase-9
Ligandability
Cysteine 172 of Caspase-9
Cysteine 256 of Caspase-9
2ar9 D 239 D 256
A redox-regulated disulphide may form within Caspase-9 between cysteines 239 and 256. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
2ar9
Structure name
crystal structure of a dimeric caspase-9
Structure deposition date
2005-08-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
56
Minimum pKa ?
9
% buried
18
Peptide accession
P55211
Residue number A
239
Residue number B
256
Peptide name
Caspase-9
Ligandability
Cysteine 239 of Caspase-9
Cysteine 256 of Caspase-9
2ar9 B 229 B 230
A redox-regulated disulphide may form within Caspase-9 between cysteines 229 and 230. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
2ar9
Structure name
crystal structure of a dimeric caspase-9
Structure deposition date
2005-08-19
Thiol separation (Å)
7
Half-sphere exposure sum ?
87
Minimum pKa ?
12
% buried
100
Peptide accession
P55211
Residue number A
229
Residue number B
230
Peptide name
Caspase-9
Ligandability
Cysteine 229 of Caspase-9
Cysteine 230 of Caspase-9
2ar9 A 163 A 230
A redox-regulated disulphide may form within Caspase-9 between cysteines 163 and 230. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
2ar9
Structure name
crystal structure of a dimeric caspase-9
Structure deposition date
2005-08-19
Thiol separation (Å)
8
Half-sphere exposure sum ?
82
Minimum pKa ?
12
% buried
99
Peptide accession
P55211
Residue number A
163
Residue number B
230
Peptide name
Caspase-9
Ligandability
Cysteine 163 of Caspase-9
Cysteine 230 of Caspase-9
3v3k I 165 I 186
A redox-regulated disulphide may form within Caspase-9 between cysteines 163 and 187 (165 and 186 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
32
PDB code
3v3k
Structure name
human caspase 9 in complex with bacterial effector protein
Structure deposition date
2011-12-13
Thiol separation (Å)
10
Half-sphere exposure sum ?
78
Minimum pKa ?
11
% buried
80
Peptide accession
P55211
Residue number A
163
Residue number B
187
Peptide name
Caspase-9
Ligandability
Cysteine 163 of Caspase-9
Cysteine 187 of Caspase-9
3v3k G 165 G 229
A redox-regulated disulphide may form within Caspase-9 between cysteines 163 and 229 (165 and 229 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
31
PDB code
3v3k
Structure name
human caspase 9 in complex with bacterial effector protein
Structure deposition date
2011-12-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
82
Minimum pKa ?
13
% buried
100
Peptide accession
P55211
Residue number A
163
Residue number B
229
Peptide name
Caspase-9
Ligandability
Cysteine 163 of Caspase-9
Cysteine 229 of Caspase-9
3v3k O 239 O 285
A redox-regulated disulphide may form within Caspase-9 between cysteines 239 and 287 (239 and 285 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
26
PDB code
3v3k
Structure name
human caspase 9 in complex with bacterial effector protein
Structure deposition date
2011-12-13
Thiol separation (Å)
10
Half-sphere exposure sum ?
86
Minimum pKa ?
10
% buried
93
Peptide accession
P55211
Residue number A
239
Residue number B
287
Peptide name
Caspase-9
Ligandability
Cysteine 239 of Caspase-9
Cysteine 287 of Caspase-9
2ar9 C 160 C 230
A redox-regulated disulphide may form within Caspase-9 between cysteines 160 and 230. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
25
PDB code
2ar9
Structure name
crystal structure of a dimeric caspase-9
Structure deposition date
2005-08-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
81
Minimum pKa ?
12
% buried
92
Peptide accession
P55211
Residue number A
160
Residue number B
230
Peptide name
Caspase-9
Ligandability
Cysteine 160 of Caspase-9
Cysteine 230 of Caspase-9
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