ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Calmodulin-regulated spectrin-associated protein 1

Intramolecular
Cysteine 1507 and cysteine 1528
Cysteine 1486 and cysteine 1487
Cysteine 1486 and cysteine 1521
Cysteine 1487 and cysteine 1521
A redox-regulated disulphide may form within Calmodulin-regulated spectrin-associated protein 1 between cysteines 1507 and 1528 (35 and 56 respectively in this structure).

Details

Redox score ?
71
PDB code
6qvj
Structure name
hsckk (human camsap1) decorated 14pf taxol-gdp microtubule
Structure deposition date
2019-03-02
Thiol separation (Å)
5
Half-sphere exposure sum ?
53
Minimum pKa ?
8
% buried
16
Peptide accession
Q5T5Y3
Residue number A
1507
Residue number B
1528
Peptide name
Calmodulin-regulated spectrin-associated protein 1

Ligandability

Cysteine 1507 of Calmodulin-regulated spectrin-associated protein 1

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 1528 of Calmodulin-regulated spectrin-associated protein 1

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 1 between cysteines 1486 and 1487 (1497 and 1498 respectively in this structure).

Details

Redox score ?
69
PDB code
5m54
Structure name
mechanism of microtubule minus-end recognition and protection by camsap proteins
Structure deposition date
2016-10-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
8
% buried
92
Peptide accession
Q5T5Y3
Residue number A
1486
Residue number B
1487
Peptide name
Calmodulin-regulated spectrin-associated protein 1

Ligandability

Cysteine 1486 of Calmodulin-regulated spectrin-associated protein 1

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 1487 of Calmodulin-regulated spectrin-associated protein 1

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 1 between cysteines 1486 and 1521 (1497 and 1532 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
6qus
Structure name
hsckk (human camsap1) decorated 13pf taxol-gdp microtubule
Structure deposition date
2019-02-28
Thiol separation (Å)
6
Half-sphere exposure sum ?
72
Minimum pKa ?
8
% buried
94
Peptide accession
Q5T5Y3
Residue number A
1486
Residue number B
1521
Peptide name
Calmodulin-regulated spectrin-associated protein 1

Ligandability

Cysteine 1486 of Calmodulin-regulated spectrin-associated protein 1

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 1521 of Calmodulin-regulated spectrin-associated protein 1

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 1 between cysteines 1487 and 1521 (1498 and 1532 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
6qus
Structure name
hsckk (human camsap1) decorated 13pf taxol-gdp microtubule
Structure deposition date
2019-02-28
Thiol separation (Å)
6
Half-sphere exposure sum ?
80
Minimum pKa ?
12
% buried
98
Peptide accession
Q5T5Y3
Residue number A
1487
Residue number B
1521
Peptide name
Calmodulin-regulated spectrin-associated protein 1

Ligandability

Cysteine 1487 of Calmodulin-regulated spectrin-associated protein 1

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 1521 of Calmodulin-regulated spectrin-associated protein 1

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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