ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Calpain-3

Intramolecular
Cysteine 697 and cysteine 784
Cysteine 669 and cysteine 697
Cysteine 784 and cysteine 785
Cysteine 137 and cysteine 264
Cysteine 137 and cysteine 414
A redox-regulated disulphide may form within Calpain-3 between cysteines 697 and 784. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
4okh
Structure name
crystal structure of calpain-3 penta-ef-hand domain
Structure deposition date
2014-01-22
Thiol separation (Å)
8
Half-sphere exposure sum ?
72
Minimum pKa ?
10
% buried
55
Peptide accession
P20807
Residue number A
697
Residue number B
784
Peptide name
Calpain-3

Ligandability

Cysteine 697 of Calpain-3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 784 of Calpain-3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Calpain-3 between cysteines 669 and 697. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
4okh
Structure name
crystal structure of calpain-3 penta-ef-hand domain
Structure deposition date
2014-01-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
69
Minimum pKa ?
9
% buried
44
Peptide accession
P20807
Residue number A
669
Residue number B
697
Peptide name
Calpain-3

Ligandability

Cysteine 669 of Calpain-3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 697 of Calpain-3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Calpain-3 between cysteines 784 and 785. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
4okh
Structure name
crystal structure of calpain-3 penta-ef-hand domain
Structure deposition date
2014-01-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
70
Minimum pKa ?
10
% buried
76
Peptide accession
P20807
Residue number A
784
Residue number B
785
Peptide name
Calpain-3

Ligandability

Cysteine 784 of Calpain-3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 785 of Calpain-3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Calpain-3 between cysteines 137 and 264. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
PDB code
6bdt
Structure name
crystal structure of human calpain-3 protease core mutant-c129s
Structure deposition date
2017-10-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
98
Minimum pKa ?
11
% buried
100
Peptide accession
P20807
Residue number A
137
Residue number B
264
Peptide name
Calpain-3

Ligandability

Cysteine 137 of Calpain-3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 264 of Calpain-3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Calpain-3 between cysteines 137 and 414. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
26
PDB code
6bgp
Structure name
crystal structure of human calpain-3 protease core mutant-c129a
Structure deposition date
2017-10-29
Thiol separation (Å)
10
Half-sphere exposure sum ?
89
Minimum pKa ?
11
% buried
98
Peptide accession
P20807
Residue number A
137
Residue number B
414
Peptide name
Calpain-3

Ligandability

Cysteine 137 of Calpain-3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 414 of Calpain-3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

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