ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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cGMP-dependent protein kinase 1

Intermolecular
Cysteine 43 and cysteine 43
Cysteine 175 and cysteine 158
Intramolecular
Cysteine 118 and cysteine 196
A redox-regulated disulphide is known to form between two units of cGMP-dependent protein kinase 1 at cysteines 43 and 43.

Details

Redox score ?
60
PDB code
1zxa
Structure name
solution structure of the coiled-coil domain of cgmp-dependent protein kinase ia
Structure deposition date
2005-06-07
Thiol separation (Å)
8
Half-sphere exposure sum ?
22
Minimum pKa ?
9
% buried
0
Peptide A name
cGMP-dependent protein kinase 1
Peptide B name
cGMP-dependent protein kinase 1
Peptide A accession
Q13976
Peptide B accession
Q13976
Peptide A residue number
43
Peptide B residue number
43

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 between two units of cGMP-dependent protein kinase 1 at cysteines 175 and 158 (190 and 173 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
3od0
Structure name
crystal structure of cgmp bound cgmp-dependent protein kinase(92-227)
Structure deposition date
2010-08-10
Thiol separation (Å)
9
Half-sphere exposure sum ?
45
Minimum pKa ?
10
% buried
48
Peptide A name
cGMP-dependent protein kinase 1
Peptide B name
cGMP-dependent protein kinase 1
Peptide A accession
Q6P5T7
Peptide B accession
Q6P5T7
Peptide A residue number
175
Peptide B residue number
158

Ligandability

Cysteine 175 of cGMP-dependent protein kinase 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 158 of cGMP-dependent protein kinase 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 cGMP-dependent protein kinase 1 between cysteines 118 and 196 (117 and 195 respectively in this structure).

Details

Redox score ?
81
PDB code
3shr
Structure name
crystal structure of cgmp-dependent protein kinase reveals novel site of interchain communication
Structure deposition date
2011-06-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00516
Residue number A
118
Residue number B
196
Peptide name
cGMP-dependent protein kinase 1

Ligandability

Cysteine 118 of cGMP-dependent protein kinase 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 196 of cGMP-dependent protein kinase 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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