ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Voltage-dependent L-type calcium channel subunit alpha-1C

Intramolecular
Cysteine 489 and cysteine 1255
Cysteine 427 and cysteine 432
A redox-regulated disulphide may form within Voltage-dependent L-type calcium channel subunit alpha-1C between cysteines 489 and 1255 (435 and 439 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
5v2q
Structure name
cav beta2a subunit: cav1
Structure deposition date
2017-03-06
Thiol separation (Å)
7
Half-sphere exposure sum ?
45
Minimum pKa ?
9
% buried
0
Peptide accession
Q13936
Residue number A
489
Residue number B
1255
Peptide name
Voltage-dependent L-type calcium channel subunit alpha-1C

Ligandability

Cysteine 489 of Voltage-dependent L-type calcium channel subunit alpha-1C

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 1255 of Voltage-dependent L-type calcium channel subunit alpha-1C

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 Voltage-dependent L-type calcium channel subunit alpha-1C between cysteines 427 and 432.

Details

Redox score ?
nan
PDB code
5v2p
Structure name
cav beta2a subunit: cav1
Structure deposition date
2017-03-06
Thiol separation (Å)
6
Half-sphere exposure sum ?
nan
Minimum pKa ?
10
% buried
nan
Peptide accession
Q13936
Residue number A
427
Residue number B
432
Peptide name
Voltage-dependent L-type calcium channel subunit alpha-1C

Ligandability

Cysteine 427 of Voltage-dependent L-type calcium channel subunit alpha-1C

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 432 of Voltage-dependent L-type calcium channel subunit alpha-1C

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 427 in protein A could not be asigned to a Uniprot residue.
Cysteine 432 in protein B could not be asigned to a Uniprot residue.
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