Caspase-3
Intermolecular
Cysteine 220 and cysteine 264
Cysteine 220 and cysteine 220
Cysteine 264 and cysteine 264
Intramolecular
Cysteine 184 and cysteine 264 L
Cysteine 47 and cysteine 116
Cysteine 47 and cysteine 220
5i9t A 266 C 264
A redox-regulated disulphide may form between two units of Caspase-3 at cysteines 220 and 264 (266 and 264 respectively in this structure).
Details
Redox score ?
69
PDB code
5i9t
Structure name
caspase 3 v266c
Structure deposition date
2016-02-20
Thiol separation (Å)
3
Half-sphere exposure sum ?
84
Minimum pKa ?
9
% buried
75
Peptide A name
Caspase-3
Peptide B name
Caspase-3
Peptide A accession
P42574
Peptide B accession
P42574
Peptide A residue number
220
Peptide B residue number
264
Ligandability
Cysteine 220 of Caspase-3
Cysteine 264 of Caspase-3
5i9t A 266 C 266
A redox-regulated disulphide may form between two units of Caspase-3 at cysteines 220 and 220 (266 and 266 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
55
PDB code
5i9t
Structure name
caspase 3 v266c
Structure deposition date
2016-02-20
Thiol separation (Å)
6
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
50
Peptide A name
Caspase-3
Peptide B name
Caspase-3
Peptide A accession
P42574
Peptide B accession
P42574
Peptide A residue number
220
Peptide B residue number
220
Ligandability
4jqy A 264 B 264
A redox-regulated disulphide may form between two units of Caspase-3 at cysteines 264 and 264. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
31
PDB code
4jqy
Structure name
human procaspase-3, crystal form 1
Structure deposition date
2013-03-20
Thiol separation (Å)
9
Half-sphere exposure sum ?
83
Minimum pKa ?
12
% buried
100
Peptide A name
Caspase-3
Peptide B name
Caspase-3
Peptide A accession
P42574
Peptide B accession
P42574
Peptide A residue number
264
Peptide B residue number
264
Ligandability
4ehn A 197 A 264
A redox-regulated disulphide may form within Caspase-3 between cysteines 184 and 264 (197 and 264 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
55
PDB code
4ehn
Structure name
allosteric modulation of caspase-3 through mutagenesis
Structure deposition date
2012-04-02
Thiol separation (Å)
6
Half-sphere exposure sum ?
75
Minimum pKa ?
8
% buried
64
Peptide accession
P42574
Residue number A
184
Residue number B
264
Peptide name
Caspase-3
Ligandability
Cysteine 184 of Caspase-3
Cysteine 264 of Caspase-3
2j33 A 47 A 116
A redox-regulated disulphide may form within Caspase-3 between cysteines 47 and 116. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
32
PDB code
2j33
Structure name
the role of loop bundle hydrogen bonds in the maturation and activity of (pro)caspase-3
Structure deposition date
2006-08-17
Thiol separation (Å)
8
Half-sphere exposure sum ?
80
Minimum pKa ?
13
% buried
100
Peptide accession
P42574
Residue number A
47
Residue number B
116
Peptide name
Caspase-3
Ligandability
Cysteine 47 of Caspase-3
Cysteine 116 of Caspase-3
4ps0 A 47 A 220
A redox-regulated disulphide may form within Caspase-3 between cysteines 47 and 220. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
31
PDB code
4ps0
Structure name
caspase-8 specific unnatural amino acid peptides
Structure deposition date
2014-03-06
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
12
% buried
96
Peptide accession
P42574
Residue number A
47
Residue number B
220
Peptide name
Caspase-3
Ligandability
Cysteine 47 of Caspase-3
Cysteine 220 of Caspase-3
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