a tool for identifying drug-targetable redox-active disulphides

High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A

Intramolecular

Cysteine 364 and cysteine 367

Cysteine 360 and cysteine 364

Cysteine 226 and cysteine 364

Cysteine 360 and cysteine 367

A redox-regulated disulphide may form within High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A between cysteines 364 and 367. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

49

PDB code

Structure name

pde7a catalytic domain in complex with 2-(cyclopentylamino)thieno[3,2- d]pyrimidin-4(3h)-one derivative

Structure deposition date

2014-05-20

Thiol separation (Å)

6

Half-sphere exposure sum ?

83

Minimum pK_a ?

12

% buried

100

Peptide accession

Residue number A

364

Residue number B

367

Peptide name

High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A

Ligandability

Cysteine 364 of High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A

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 367 of High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A

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 High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A between cysteines 360 and 364. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

36

PDB code

Structure name

pde7a catalytic domain in complex with 3-(2,6- difluorophenyl)-2-(methylthio)quinazolin-4(3h)-one

Structure deposition date

2009-02-02

Thiol separation (Å)

8

Half-sphere exposure sum ?

90

Minimum pK_a ?

12

% buried

100

Peptide accession

Residue number A

360

Residue number B

364

Peptide name

High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A

Ligandability

Cysteine 360 of High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A

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 364 of High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A

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 High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A between cysteines 226 and 364. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

36

PDB code

Structure name

pde7a catalytic domain in complex with 3-(2,6- difluorophenyl)-2-(methylthio)quinazolin-4(3h)-one

Structure deposition date

2009-02-02

Thiol separation (Å)

9

Half-sphere exposure sum ?

78

Minimum pK_a ?

11

% buried

98

Peptide accession

Residue number A

226

Residue number B

364

Peptide name

High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A

Ligandability

Cysteine 226 of High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A

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 364 of High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A

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 High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A between cysteines 360 and 367. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

35

PDB code

Structure name

pde7a catalytic domain in complex with 2-(cyclopentylamino)thieno[3,2- d]pyrimidin-4(3h)-one derivative

Structure deposition date

2014-05-20

Thiol separation (Å)

8

Half-sphere exposure sum ?

85

Minimum pK_a ?

13

% buried

100

Peptide accession

Residue number A

360

Residue number B

367

Peptide name

High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A

Ligandability

Cysteine 360 of High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A

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 367 of High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A

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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