Caspase-8
Intermolecular
Cysteine 2 of Early 35 kDa protein and cysteine 360 L
Cysteine 313 and cysteine 426
Cysteine 360 and cysteine 409 L
Intramolecular
Cysteine 236 and cysteine 313
Cysteine 312 and cysteine 313
Cysteine 309 and cysteine 433
Cysteine 236 and cysteine 433
Cysteine 236 and cysteine 426
Cysteine 312 and cysteine 345
Cysteine 236 and cysteine 309
More...Cysteine 426 and cysteine 433
Cysteine 236 and cysteine 312
Cysteine 287 and cysteine 312
1i4e A 2 B 2360
A redox-regulated disulphide may form between cysteine 2 of Early 35 kDa protein and cysteine 360 of Caspase-8 (2 and 2360 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
58
PDB code
1i4e
Structure name
crystal structure of the caspase-8/p35 complex
Structure deposition date
2001-02-20
Thiol separation (Å)
6
Half-sphere exposure sum ?
nan
Minimum pKa ?
10
% buried
84
Peptide A name
Early 35 kDa protein
Peptide B name
Caspase-8
Peptide A accession
P08160
Peptide B accession
Q14790
Peptide A residue number
2
Peptide B residue number
360
Ligandability
Cysteine 2 of Early 35 kDa protein
Cysteine 360 of Caspase-8
2y1l C 313 D 426
A redox-regulated disulphide may form between two units of Caspase-8 at cysteines 313 and 426. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
2y1l
Structure name
caspase-8 in complex with darpin-8
Structure deposition date
2010-12-08
Thiol separation (Å)
7
Half-sphere exposure sum ?
84
Minimum pKa ?
10
% buried
100
Peptide A name
Caspase-8
Peptide B name
Caspase-8
Peptide A accession
Q14790
Peptide B accession
Q14790
Peptide A residue number
313
Peptide B residue number
426
Ligandability
Cysteine 313 of Caspase-8
Cysteine 426 of Caspase-8
3kjn A 360 B 409
A redox-regulated disulphide may form between two units of Caspase-8 at cysteines 360 and 409. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
3kjn
Structure name
caspase 8 bound to a covalent inhibitor
Structure deposition date
2009-11-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
66
Minimum pKa ?
9
% buried
62
Peptide A name
Caspase-8
Peptide B name
Caspase-8
Peptide A accession
Q14790
Peptide B accession
Q14790
Peptide A residue number
360
Peptide B residue number
409
Ligandability
Cysteine 360 of Caspase-8
Cysteine 409 of Caspase-8
6px9 C 236 C 313
A redox-regulated disulphide may form within Caspase-8 between cysteines 236 and 313.
Details
Redox score ?
64
PDB code
6px9
Structure name
crystal structure of procaspase-8 in complex with covalent small molecule inhibitor 63-r
Structure deposition date
2019-07-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
81
Minimum pKa ?
9
% buried
100
Peptide accession
Q14790
Residue number A
236
Residue number B
313
Peptide name
Caspase-8
Ligandability
Cysteine 236 of Caspase-8
Cysteine 313 of Caspase-8
1qdu E 232 E 233
A redox-regulated disulphide may form within Caspase-8 between cysteines 312 and 313 (232 and 233 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
1qdu
Structure name
crystal structure of the complex of caspase-8 with the tripeptide ketone inhibitor zevd-dcbmk
Structure deposition date
1999-07-10
Thiol separation (Å)
6
Half-sphere exposure sum ?
87
Minimum pKa ?
9
% buried
100
Peptide accession
Q14790
Residue number A
312
Residue number B
313
Peptide name
Caspase-8
Ligandability
Cysteine 312 of Caspase-8
Cysteine 313 of Caspase-8
2k7z A 309 A 433
A redox-regulated disulphide may form within Caspase-8 between cysteines 309 and 433. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
2k7z
Structure name
solution structure of the catalytic domain of procaspase-8
Structure deposition date
2008-08-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
68
Minimum pKa ?
11
% buried
66
Peptide accession
Q14790
Residue number A
309
Residue number B
433
Peptide name
Caspase-8
Ligandability
Cysteine 309 of Caspase-8
Cysteine 433 of Caspase-8
2k7z A 236 A 433
A redox-regulated disulphide may form within Caspase-8 between cysteines 236 and 433. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
2k7z
Structure name
solution structure of the catalytic domain of procaspase-8
Structure deposition date
2008-08-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
61
Minimum pKa ?
11
% buried
70
Peptide accession
Q14790
Residue number A
236
Residue number B
433
Peptide name
Caspase-8
Ligandability
Cysteine 236 of Caspase-8
Cysteine 433 of Caspase-8
6px9 F 236 F 426
A redox-regulated disulphide may form within Caspase-8 between cysteines 236 and 426. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
6px9
Structure name
crystal structure of procaspase-8 in complex with covalent small molecule inhibitor 63-r
Structure deposition date
2019-07-25
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
10
% buried
90
Peptide accession
Q14790
Residue number A
236
Residue number B
426
Peptide name
Caspase-8
Ligandability
Cysteine 236 of Caspase-8
Cysteine 426 of Caspase-8
2k7z A 312 A 345
A redox-regulated disulphide may form within Caspase-8 between cysteines 312 and 345. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
2k7z
Structure name
solution structure of the catalytic domain of procaspase-8
Structure deposition date
2008-08-28
Thiol separation (Å)
10
Half-sphere exposure sum ?
46
Minimum pKa ?
9
% buried
48
Peptide accession
Q14790
Residue number A
312
Residue number B
345
Peptide name
Caspase-8
Ligandability
Cysteine 312 of Caspase-8
Cysteine 345 of Caspase-8
1qdu G 165 G 229
A redox-regulated disulphide may form within Caspase-8 between cysteines 236 and 309 (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 ?
38
PDB code
1qdu
Structure name
crystal structure of the complex of caspase-8 with the tripeptide ketone inhibitor zevd-dcbmk
Structure deposition date
1999-07-10
Thiol separation (Å)
9
Half-sphere exposure sum ?
79
Minimum pKa ?
10
% buried
100
Peptide accession
Q14790
Residue number A
236
Residue number B
309
Peptide name
Caspase-8
Ligandability
Cysteine 236 of Caspase-8
Cysteine 309 of Caspase-8
2fun B 2426 B 2433
A redox-regulated disulphide may form within Caspase-8 between cysteines 426 and 433 (2426 and 2433 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
33
PDB code
2fun
Structure name
alternative p35-caspase-8 complex
Structure deposition date
2006-01-27
Thiol separation (Å)
10
Half-sphere exposure sum ?
66
Minimum pKa ?
12
% buried
84
Peptide accession
Q14790
Residue number A
426
Residue number B
433
Peptide name
Caspase-8
Ligandability
Cysteine 426 of Caspase-8
Cysteine 433 of Caspase-8
1qdu E 165 E 232
A redox-regulated disulphide may form within Caspase-8 between cysteines 236 and 312 (165 and 232 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
1qdu
Structure name
crystal structure of the complex of caspase-8 with the tripeptide ketone inhibitor zevd-dcbmk
Structure deposition date
1999-07-10
Thiol separation (Å)
8
Half-sphere exposure sum ?
80
Minimum pKa ?
13
% buried
100
Peptide accession
Q14790
Residue number A
236
Residue number B
312
Peptide name
Caspase-8
Ligandability
Cysteine 236 of Caspase-8
Cysteine 312 of Caspase-8
4ps1 A 287 A 312
A redox-regulated disulphide may form within Caspase-8 between cysteines 287 and 312. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
20
PDB code
4ps1
Structure name
caspase-8 specific unnatural amino acid peptides
Structure deposition date
2014-03-06
Thiol separation (Å)
10
Half-sphere exposure sum ?
86
Minimum pKa ?
13
% buried
100
Peptide accession
Q14790
Residue number A
287
Residue number B
312
Peptide name
Caspase-8
Ligandability
Cysteine 287 of Caspase-8
Cysteine 312 of Caspase-8
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