ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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cAMP-dependent protein kinase type I-beta regulatory subunit

Intermolecular
Cysteine 18 and cysteine 39
Cysteine 34 and cysteine 34
Intramolecular
Cysteine 34 and cysteine 39
A redox-regulated disulphide may form between two units of cAMP-dependent protein kinase type I-beta regulatory subunit at cysteines 18 and 39.

Details

Redox score ?
87
PDB code
4f9k
Structure name
crystal structure of human camp-dependent protein kinase type i-beta regulatory subunit (fragment 11-73), northeast structural genomics consortium (nesg) target hr8613a
Structure deposition date
2012-05-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
47
Minimum pKa ?
nan
% buried
nan
Peptide A name
cAMP-dependent protein kinase type I-beta regulatory subunit
Peptide B name
cAMP-dependent protein kinase type I-beta regulatory subunit
Peptide A accession
P31321
Peptide B accession
P31321
Peptide A residue number
18
Peptide B residue number
39

Ligandability

Cysteine 18 of cAMP-dependent protein kinase type I-beta 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 39 of cAMP-dependent protein kinase type I-beta 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 between two units of cAMP-dependent protein kinase type I-beta regulatory subunit at cysteines 34 and 34. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
4f9k
Structure name
crystal structure of human camp-dependent protein kinase type i-beta regulatory subunit (fragment 11-73), northeast structural genomics consortium (nesg) target hr8613a
Structure deposition date
2012-05-18
Thiol separation (Å)
8
Half-sphere exposure sum ?
59
Minimum pKa ?
12
% buried
78
Peptide A name
cAMP-dependent protein kinase type I-beta regulatory subunit
Peptide B name
cAMP-dependent protein kinase type I-beta regulatory subunit
Peptide A accession
P31321
Peptide B accession
P31321
Peptide A residue number
34
Peptide B residue number
34

Ligandability

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 I-beta regulatory subunit between cysteines 34 and 39. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
4f9k
Structure name
crystal structure of human camp-dependent protein kinase type i-beta regulatory subunit (fragment 11-73), northeast structural genomics consortium (nesg) target hr8613a
Structure deposition date
2012-05-18
Thiol separation (Å)
10
Half-sphere exposure sum ?
52
Minimum pKa ?
12
% buried
nan
Peptide accession
P31321
Residue number A
34
Residue number B
39
Peptide name
cAMP-dependent protein kinase type I-beta regulatory subunit

Ligandability

Cysteine 34 of cAMP-dependent protein kinase type I-beta 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 39 of cAMP-dependent protein kinase type I-beta 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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