ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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cAMP-dependent protein kinase type II-alpha regulatory subunit

Intermolecular
Cysteine 200 of cAMP-dependent protein kinase catalytic subunit alpha and cysteine 98
Intramolecular
Cysteine 327 and cysteine 356
A redox-regulated disulphide may form between cysteine 200 of cAMP-dependent protein kinase catalytic subunit alpha and cysteine 98 of cAMP-dependent protein kinase type II-alpha regulatory subunit (199 and 97 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
2qvs
Structure name
crystal structure of type iia holoenzyme of camp-dependent protein kinase
Structure deposition date
2007-08-08
Thiol separation (Å)
5
Half-sphere exposure sum ?
67
Minimum pKa ?
11
% buried
87
Peptide A name
cAMP-dependent protein kinase catalytic subunit alpha
Peptide B name
cAMP-dependent protein kinase type II-alpha regulatory subunit
Peptide A accession
P05132
Peptide B accession
P12367
Peptide A residue number
200
Peptide B residue number
98

Ligandability

Cysteine 200 of cAMP-dependent protein kinase catalytic subunit alpha

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 98 of cAMP-dependent protein kinase type II-alpha regulatory subunit

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 cAMP-dependent protein kinase type II-alpha regulatory subunit between cysteines 327 and 356 (326 and 355 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
2qvs
Structure name
crystal structure of type iia holoenzyme of camp-dependent protein kinase
Structure deposition date
2007-08-08
Thiol separation (Å)
9
Half-sphere exposure sum ?
67
Minimum pKa ?
11
% buried
62
Peptide accession
P12367
Residue number A
327
Residue number B
356
Peptide name
cAMP-dependent protein kinase type II-alpha regulatory subunit

Ligandability

Cysteine 327 of cAMP-dependent protein kinase type II-alpha regulatory subunit

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 356 of cAMP-dependent protein kinase type II-alpha regulatory subunit

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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