ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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cGMP-inhibited 3',5'-cyclic phosphodiesterase 3B

Intramolecular
Cysteine 792 and cysteine 801
Cysteine 1000 and cysteine 1059
Cysteine 929 and cysteine 932
A redox-regulated disulphide may form within cGMP-inhibited 3',5'-cyclic phosphodiesterase 3B between cysteines 792 and 801. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
1so2
Structure name
catalytic domain of human phosphodiesterase 3b in complex with a dihydropyridazine inhibitor
Structure deposition date
2004-03-12
Thiol separation (Å)
7
Half-sphere exposure sum ?
66
Minimum pKa ?
8
% buried
62
Peptide accession
Q13370
Residue number A
792
Residue number B
801
Peptide name
cGMP-inhibited 3',5'-cyclic phosphodiesterase 3B

Ligandability

Cysteine 792 of cGMP-inhibited 3',5'-cyclic phosphodiesterase 3B

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 801 of cGMP-inhibited 3',5'-cyclic phosphodiesterase 3B

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-inhibited 3',5'-cyclic phosphodiesterase 3B between cysteines 1000 and 1059. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
1so2
Structure name
catalytic domain of human phosphodiesterase 3b in complex with a dihydropyridazine inhibitor
Structure deposition date
2004-03-12
Thiol separation (Å)
8
Half-sphere exposure sum ?
69
Minimum pKa ?
11
% buried
88
Peptide accession
Q13370
Residue number A
1000
Residue number B
1059
Peptide name
cGMP-inhibited 3',5'-cyclic phosphodiesterase 3B

Ligandability

Cysteine 1000 of cGMP-inhibited 3',5'-cyclic phosphodiesterase 3B

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 1059 of cGMP-inhibited 3',5'-cyclic phosphodiesterase 3B

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-inhibited 3',5'-cyclic phosphodiesterase 3B between cysteines 929 and 932. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
1soj
Structure name
catalytic domain of human phosphodiesterase 3b in complex with ibmx
Structure deposition date
2004-03-15
Thiol separation (Å)
7
Half-sphere exposure sum ?
90
Minimum pKa ?
12
% buried
100
Peptide accession
Q13370
Residue number A
929
Residue number B
932
Peptide name
cGMP-inhibited 3',5'-cyclic phosphodiesterase 3B

Ligandability

Cysteine 929 of cGMP-inhibited 3',5'-cyclic phosphodiesterase 3B

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 932 of cGMP-inhibited 3',5'-cyclic phosphodiesterase 3B

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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