ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Protein kinase, cAMP dependent regulatory, type II alpha

Intermolecular
Cysteine 99 and cysteine 200 of cAMP-dependent protein kinase catalytic subunit alpha
Intramolecular
Cysteine 328 and cysteine 357
A redox-regulated disulphide may form between cysteine 99 of Protein kinase, cAMP dependent regulatory, type II alpha and cysteine 200 of cAMP-dependent protein kinase catalytic subunit alpha (99 and 199 respectively in this structure).

Details

Redox score ?
61
PDB code
3j4r
Structure name
pseudo-atomic model of the akap18-pka complex in a linear conformation derived from electron microscopy
Structure deposition date
2013-09-25
Thiol separation (Å)
5
Half-sphere exposure sum ?
69
Minimum pKa ?
10
% buried
86
Peptide A name
Protein kinase, cAMP dependent regulatory, type II alpha
Peptide B name
cAMP-dependent protein kinase catalytic subunit alpha
Peptide A accession
Q8K1M3
Peptide B accession
P05132
Peptide A residue number
99
Peptide B residue number
200

Ligandability

Cysteine 99 of Protein kinase, cAMP dependent regulatory, type II alpha

Cysteine 200 of cAMP-dependent protein kinase catalytic subunit alpha

A redox-regulated disulphide may form within Protein kinase, cAMP dependent regulatory, type II alpha between cysteines 328 and 357. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
3j4r
Structure name
pseudo-atomic model of the akap18-pka complex in a linear conformation derived from electron microscopy
Structure deposition date
2013-09-25
Thiol separation (Å)
9
Half-sphere exposure sum ?
67
Minimum pKa ?
11
% buried
62
Peptide accession
Q8K1M3
Residue number A
328
Residue number B
357
Peptide name
Protein kinase, cAMP dependent regulatory, type II alpha

Ligandability

Cysteine 328 of Protein kinase, cAMP dependent regulatory, type II alpha

Cysteine 357 of Protein kinase, cAMP dependent regulatory, type II alpha

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