ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Calmodulin-regulated spectrin-associated protein 3

Intramolecular
Cysteine 1135 and cysteine 1136
Cysteine 1135 and cysteine 1170
Cysteine 1136 and cysteine 1170
A redox-regulated disulphide may form within Calmodulin-regulated spectrin-associated protein 3 between cysteines 1135 and 1136.

Details

Redox score ?
68
PDB code
5lzn
Structure name
-tip microtubule-binding domain
Structure deposition date
2016-09-30
Thiol separation (Å)
5
Half-sphere exposure sum ?
55
Minimum pKa ?
10
% buried
54
Peptide accession
Q80VC9
Residue number A
1135
Residue number B
1136
Peptide name
Calmodulin-regulated spectrin-associated protein 3

Ligandability

Cysteine 1135 of Calmodulin-regulated spectrin-associated protein 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 1136 of Calmodulin-regulated spectrin-associated protein 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 Calmodulin-regulated spectrin-associated protein 3 between cysteines 1135 and 1170. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
5lzn
Structure name
-tip microtubule-binding domain
Structure deposition date
2016-09-30
Thiol separation (Å)
8
Half-sphere exposure sum ?
55
Minimum pKa ?
10
% buried
34
Peptide accession
Q80VC9
Residue number A
1135
Residue number B
1170
Peptide name
Calmodulin-regulated spectrin-associated protein 3

Ligandability

Cysteine 1135 of Calmodulin-regulated spectrin-associated protein 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 1170 of Calmodulin-regulated spectrin-associated protein 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 Calmodulin-regulated spectrin-associated protein 3 between cysteines 1136 and 1170. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
5lzn
Structure name
-tip microtubule-binding domain
Structure deposition date
2016-09-30
Thiol separation (Å)
8
Half-sphere exposure sum ?
62
Minimum pKa ?
11
% buried
56
Peptide accession
Q80VC9
Residue number A
1136
Residue number B
1170
Peptide name
Calmodulin-regulated spectrin-associated protein 3

Ligandability

Cysteine 1136 of Calmodulin-regulated spectrin-associated protein 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 1170 of Calmodulin-regulated spectrin-associated protein 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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