cGMP-dependent 3',5'-cyclic phosphodiesterase
Intermolecular
Cysteine 393 and cysteine 393
Cysteine 234 and cysteine 234
Cysteine 393 and cysteine 391
Intramolecular
Cysteine 263 and cysteine 276
Cysteine 668 and cysteine 693
Cysteine 668 and cysteine 807
Cysteine 263 and cysteine 348
Cysteine 327 and cysteine 343
Cysteine 262 and cysteine 263
Cysteine 693 and cysteine 807
More...Cysteine 300 and cysteine 327
Cysteine 636 and cysteine 643
Cysteine 263 and cysteine 332
Cysteine 693 and cysteine 695
Cysteine 234 and cysteine 369
Cysteine 295 and cysteine 332
Cysteine 430 and cysteine 544
Cysteine 430 and cysteine 504
Cysteine 262 and cysteine 348
Cysteine 643 and cysteine 743
Cysteine 643 and cysteine 695
Cysteine 276 and cysteine 348
Cysteine 262 and cysteine 369
3ibj A 393 B 393
A redox-regulated disulphide may form between two units of cGMP-dependent 3',5'-cyclic phosphodiesterase at cysteines 393 and 393.
Details
Redox score ?
65
PDB code
3ibj
Structure name
x-ray structure of pde2a
Structure deposition date
2009-07-16
Thiol separation (Å)
5
Half-sphere exposure sum ?
61
Minimum pKa ?
10
% buried
44
Peptide A name
cGMP-dependent 3',5'-cyclic phosphodiesterase
Peptide B name
cGMP-dependent 3',5'-cyclic phosphodiesterase
Peptide A accession
O00408
Peptide B accession
O00408
Peptide A residue number
393
Peptide B residue number
393
Ligandability
3ibj A 234 B 234
A redox-regulated disulphide may form between two units of cGMP-dependent 3',5'-cyclic phosphodiesterase at cysteines 234 and 234. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
56
PDB code
3ibj
Structure name
x-ray structure of pde2a
Structure deposition date
2009-07-16
Thiol separation (Å)
6
Half-sphere exposure sum ?
78
Minimum pKa ?
12
% buried
100
Peptide A name
cGMP-dependent 3',5'-cyclic phosphodiesterase
Peptide B name
cGMP-dependent 3',5'-cyclic phosphodiesterase
Peptide A accession
O00408
Peptide B accession
O00408
Peptide A residue number
234
Peptide B residue number
234
Ligandability
3ibj A 393 B 391
A redox-regulated disulphide may form between two units of cGMP-dependent 3',5'-cyclic phosphodiesterase at cysteines 393 and 391. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
3ibj
Structure name
x-ray structure of pde2a
Structure deposition date
2009-07-16
Thiol separation (Å)
8
Half-sphere exposure sum ?
52
Minimum pKa ?
9
% buried
24
Peptide A name
cGMP-dependent 3',5'-cyclic phosphodiesterase
Peptide B name
cGMP-dependent 3',5'-cyclic phosphodiesterase
Peptide A accession
O00408
Peptide B accession
O00408
Peptide A residue number
393
Peptide B residue number
391
Ligandability
Cysteine 393 of cGMP-dependent 3',5'-cyclic phosphodiesterase
Cysteine 391 of cGMP-dependent 3',5'-cyclic phosphodiesterase
3ibj B 263 B 276
A redox-regulated disulphide may form within cGMP-dependent 3',5'-cyclic phosphodiesterase between cysteines 263 and 276.
Details
Redox score ?
78
PDB code
3ibj
Structure name
x-ray structure of pde2a
Structure deposition date
2009-07-16
Thiol separation (Å)
3
Half-sphere exposure sum ?
77
Minimum pKa ?
5
% buried
96
Peptide accession
O00408
Residue number A
263
Residue number B
276
Peptide name
cGMP-dependent 3',5'-cyclic phosphodiesterase
Ligandability
Cysteine 263 of cGMP-dependent 3',5'-cyclic phosphodiesterase
Cysteine 276 of cGMP-dependent 3',5'-cyclic phosphodiesterase
6c7f A 668 A 693
A redox-regulated disulphide may form within cGMP-dependent 3',5'-cyclic phosphodiesterase between cysteines 668 and 693.
Details
Redox score ?
70
PDB code
6c7f
Structure name
crystal structure of human phosphodiesterase 2a with 1-(2-chloro-5- isobutoxy-phenyl)-n,4-dimethyl-[1,2,4]triazolo[4,3-a]quinoxaline-8- carboxamide
Structure deposition date
2018-01-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
89
Minimum pKa ?
5
% buried
100
Peptide accession
O00408
Residue number A
668
Residue number B
693
Peptide name
cGMP-dependent 3',5'-cyclic phosphodiesterase
Ligandability
Cysteine 668 of cGMP-dependent 3',5'-cyclic phosphodiesterase
Cysteine 693 of cGMP-dependent 3',5'-cyclic phosphodiesterase
4htz A 668 A 807
A redox-regulated disulphide may form within cGMP-dependent 3',5'-cyclic phosphodiesterase between cysteines 668 and 807.
Details
Redox score ?
67
PDB code
4htz
Structure name
crystal structure of pde2 catalytic domain in space group p1
Structure deposition date
2012-11-02
Thiol separation (Å)
5
Half-sphere exposure sum ?
85
Minimum pKa ?
5
% buried
100
Peptide accession
O00408
Residue number A
668
Residue number B
807
Peptide name
cGMP-dependent 3',5'-cyclic phosphodiesterase
Ligandability
Cysteine 668 of cGMP-dependent 3',5'-cyclic phosphodiesterase
Cysteine 807 of cGMP-dependent 3',5'-cyclic phosphodiesterase
3ibj A 263 A 348
A redox-regulated disulphide may form within cGMP-dependent 3',5'-cyclic phosphodiesterase between cysteines 263 and 348.
Details
Redox score ?
67
PDB code
3ibj
Structure name
x-ray structure of pde2a
Structure deposition date
2009-07-16
Thiol separation (Å)
5
Half-sphere exposure sum ?
87
Minimum pKa ?
5
% buried
100
Peptide accession
O00408
Residue number A
263
Residue number B
348
Peptide name
cGMP-dependent 3',5'-cyclic phosphodiesterase
Ligandability
Cysteine 263 of cGMP-dependent 3',5'-cyclic phosphodiesterase
Cysteine 348 of cGMP-dependent 3',5'-cyclic phosphodiesterase
1mc0 A 325 A 341
A redox-regulated disulphide may form within cGMP-dependent 3',5'-cyclic phosphodiesterase between cysteines 327 and 343 (325 and 341 respectively in this structure).
Details
Redox score ?
66
PDB code
1mc0
Structure name
regulatory segment of mouse 3',5'-cyclic nucleotide phosphodiesterase 2a, containing the gaf a and gaf b domains
Structure deposition date
2002-08-04
Thiol separation (Å)
4
Half-sphere exposure sum ?
87
Minimum pKa ?
9
% buried
100
Peptide accession
Q922S4
Residue number A
327
Residue number B
343
Peptide name
cGMP-dependent 3',5'-cyclic phosphodiesterase
Ligandability
Cysteine 327 of cGMP-dependent 3',5'-cyclic phosphodiesterase
Cysteine 343 of cGMP-dependent 3',5'-cyclic phosphodiesterase
3ibj A 262 A 263
A redox-regulated disulphide may form within cGMP-dependent 3',5'-cyclic phosphodiesterase between cysteines 262 and 263. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
55
PDB code
3ibj
Structure name
x-ray structure of pde2a
Structure deposition date
2009-07-16
Thiol separation (Å)
7
Half-sphere exposure sum ?
85
Minimum pKa ?
5
% buried
100
Peptide accession
O00408
Residue number A
262
Residue number B
263
Peptide name
cGMP-dependent 3',5'-cyclic phosphodiesterase
Ligandability
Cysteine 262 of cGMP-dependent 3',5'-cyclic phosphodiesterase
Cysteine 263 of cGMP-dependent 3',5'-cyclic phosphodiesterase
3itm C 693 C 807
A redox-regulated disulphide may form within cGMP-dependent 3',5'-cyclic phosphodiesterase between cysteines 693 and 807. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
53
PDB code
3itm
Structure name
catalytic domain of hpde2a
Structure deposition date
2009-08-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
93
Minimum pKa ?
14
% buried
100
Peptide accession
O00408
Residue number A
693
Residue number B
807
Peptide name
cGMP-dependent 3',5'-cyclic phosphodiesterase
Ligandability
Cysteine 693 of cGMP-dependent 3',5'-cyclic phosphodiesterase
Cysteine 807 of cGMP-dependent 3',5'-cyclic phosphodiesterase
1mc0 A 298 A 325
A redox-regulated disulphide may form within cGMP-dependent 3',5'-cyclic phosphodiesterase between cysteines 300 and 327 (298 and 325 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
1mc0
Structure name
regulatory segment of mouse 3',5'-cyclic nucleotide phosphodiesterase 2a, containing the gaf a and gaf b domains
Structure deposition date
2002-08-04
Thiol separation (Å)
8
Half-sphere exposure sum ?
79
Minimum pKa ?
9
% buried
74
Peptide accession
Q922S4
Residue number A
300
Residue number B
327
Peptide name
cGMP-dependent 3',5'-cyclic phosphodiesterase
Ligandability
Cysteine 300 of cGMP-dependent 3',5'-cyclic phosphodiesterase
Cysteine 327 of cGMP-dependent 3',5'-cyclic phosphodiesterase
4d09 D 636 D 643
A redox-regulated disulphide may form within cGMP-dependent 3',5'-cyclic phosphodiesterase between cysteines 636 and 643. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
4d09
Structure name
pde2a catalytic domain in complex with a brain penetrant inhibitor
Structure deposition date
2014-04-24
Thiol separation (Å)
8
Half-sphere exposure sum ?
63
Minimum pKa ?
10
% buried
58
Peptide accession
O00408
Residue number A
636
Residue number B
643
Peptide name
cGMP-dependent 3',5'-cyclic phosphodiesterase
Ligandability
Cysteine 636 of cGMP-dependent 3',5'-cyclic phosphodiesterase
Cysteine 643 of cGMP-dependent 3',5'-cyclic phosphodiesterase
3ibj B 263 B 332
A redox-regulated disulphide may form within cGMP-dependent 3',5'-cyclic phosphodiesterase between cysteines 263 and 332. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
3ibj
Structure name
x-ray structure of pde2a
Structure deposition date
2009-07-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
84
Minimum pKa ?
5
% buried
100
Peptide accession
O00408
Residue number A
263
Residue number B
332
Peptide name
cGMP-dependent 3',5'-cyclic phosphodiesterase
Ligandability
Cysteine 263 of cGMP-dependent 3',5'-cyclic phosphodiesterase
Cysteine 332 of cGMP-dependent 3',5'-cyclic phosphodiesterase
3ibj B 693 B 695
A redox-regulated disulphide may form within cGMP-dependent 3',5'-cyclic phosphodiesterase between cysteines 693 and 695. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
3ibj
Structure name
x-ray structure of pde2a
Structure deposition date
2009-07-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
98
Minimum pKa ?
6
% buried
100
Peptide accession
O00408
Residue number A
693
Residue number B
695
Peptide name
cGMP-dependent 3',5'-cyclic phosphodiesterase
Ligandability
Cysteine 693 of cGMP-dependent 3',5'-cyclic phosphodiesterase
Cysteine 695 of cGMP-dependent 3',5'-cyclic phosphodiesterase
3ibj B 234 B 369
A redox-regulated disulphide may form within cGMP-dependent 3',5'-cyclic phosphodiesterase between cysteines 234 and 369. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
3ibj
Structure name
x-ray structure of pde2a
Structure deposition date
2009-07-16
Thiol separation (Å)
8
Half-sphere exposure sum ?
79
Minimum pKa ?
12
% buried
100
Peptide accession
O00408
Residue number A
234
Residue number B
369
Peptide name
cGMP-dependent 3',5'-cyclic phosphodiesterase
Ligandability
Cysteine 234 of cGMP-dependent 3',5'-cyclic phosphodiesterase
Cysteine 369 of cGMP-dependent 3',5'-cyclic phosphodiesterase
3ibj B 295 B 332
A redox-regulated disulphide may form within cGMP-dependent 3',5'-cyclic phosphodiesterase between cysteines 295 and 332. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
3ibj
Structure name
x-ray structure of pde2a
Structure deposition date
2009-07-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
66
Minimum pKa ?
9
% buried
56
Peptide accession
O00408
Residue number A
295
Residue number B
332
Peptide name
cGMP-dependent 3',5'-cyclic phosphodiesterase
Ligandability
Cysteine 295 of cGMP-dependent 3',5'-cyclic phosphodiesterase
Cysteine 332 of cGMP-dependent 3',5'-cyclic phosphodiesterase
3ibj A 430 A 544
A redox-regulated disulphide may form within cGMP-dependent 3',5'-cyclic phosphodiesterase between cysteines 430 and 544. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
3ibj
Structure name
x-ray structure of pde2a
Structure deposition date
2009-07-16
Thiol separation (Å)
8
Half-sphere exposure sum ?
79
Minimum pKa ?
12
% buried
98
Peptide accession
O00408
Residue number A
430
Residue number B
544
Peptide name
cGMP-dependent 3',5'-cyclic phosphodiesterase
Ligandability
Cysteine 430 of cGMP-dependent 3',5'-cyclic phosphodiesterase
Cysteine 544 of cGMP-dependent 3',5'-cyclic phosphodiesterase
3ibj A 430 A 504
A redox-regulated disulphide may form within cGMP-dependent 3',5'-cyclic phosphodiesterase between cysteines 430 and 504. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
35
PDB code
3ibj
Structure name
x-ray structure of pde2a
Structure deposition date
2009-07-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
74
Minimum pKa ?
12
% buried
97
Peptide accession
O00408
Residue number A
430
Residue number B
504
Peptide name
cGMP-dependent 3',5'-cyclic phosphodiesterase
Ligandability
Cysteine 430 of cGMP-dependent 3',5'-cyclic phosphodiesterase
Cysteine 504 of cGMP-dependent 3',5'-cyclic phosphodiesterase
3ibj B 262 B 348
A redox-regulated disulphide may form within cGMP-dependent 3',5'-cyclic phosphodiesterase between cysteines 262 and 348. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
3ibj
Structure name
x-ray structure of pde2a
Structure deposition date
2009-07-16
Thiol separation (Å)
8
Half-sphere exposure sum ?
85
Minimum pKa ?
12
% buried
100
Peptide accession
O00408
Residue number A
262
Residue number B
348
Peptide name
cGMP-dependent 3',5'-cyclic phosphodiesterase
Ligandability
Cysteine 262 of cGMP-dependent 3',5'-cyclic phosphodiesterase
Cysteine 348 of cGMP-dependent 3',5'-cyclic phosphodiesterase
6cyd B 643 B 743
A redox-regulated disulphide may form within cGMP-dependent 3',5'-cyclic phosphodiesterase between cysteines 643 and 743. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
6cyd
Structure name
pde2 in complex with compound 7
Structure deposition date
2018-04-05
Thiol separation (Å)
10
Half-sphere exposure sum ?
69
Minimum pKa ?
10
% buried
68
Peptide accession
O00408
Residue number A
643
Residue number B
743
Peptide name
cGMP-dependent 3',5'-cyclic phosphodiesterase
Ligandability
Cysteine 643 of cGMP-dependent 3',5'-cyclic phosphodiesterase
Cysteine 743 of cGMP-dependent 3',5'-cyclic phosphodiesterase
3itm A 643 A 695
A redox-regulated disulphide may form within cGMP-dependent 3',5'-cyclic phosphodiesterase between cysteines 643 and 695. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
29
PDB code
3itm
Structure name
catalytic domain of hpde2a
Structure deposition date
2009-08-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
88
Minimum pKa ?
13
% buried
100
Peptide accession
O00408
Residue number A
643
Residue number B
695
Peptide name
cGMP-dependent 3',5'-cyclic phosphodiesterase
Ligandability
Cysteine 643 of cGMP-dependent 3',5'-cyclic phosphodiesterase
Cysteine 695 of cGMP-dependent 3',5'-cyclic phosphodiesterase
3ibj A 276 A 348
A redox-regulated disulphide may form within cGMP-dependent 3',5'-cyclic phosphodiesterase between cysteines 276 and 348. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
29
PDB code
3ibj
Structure name
x-ray structure of pde2a
Structure deposition date
2009-07-16
Thiol separation (Å)
8
Half-sphere exposure sum ?
75
Minimum pKa ?
17
% buried
92
Peptide accession
O00408
Residue number A
276
Residue number B
348
Peptide name
cGMP-dependent 3',5'-cyclic phosphodiesterase
Ligandability
Cysteine 276 of cGMP-dependent 3',5'-cyclic phosphodiesterase
Cysteine 348 of cGMP-dependent 3',5'-cyclic phosphodiesterase
3ibj A 262 A 369
A redox-regulated disulphide may form within cGMP-dependent 3',5'-cyclic phosphodiesterase between cysteines 262 and 369. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
27
PDB code
3ibj
Structure name
x-ray structure of pde2a
Structure deposition date
2009-07-16
Thiol separation (Å)
10
Half-sphere exposure sum ?
82
Minimum pKa ?
13
% buried
100
Peptide accession
O00408
Residue number A
262
Residue number B
369
Peptide name
cGMP-dependent 3',5'-cyclic phosphodiesterase
Ligandability
Cysteine 262 of cGMP-dependent 3',5'-cyclic phosphodiesterase
Cysteine 369 of cGMP-dependent 3',5'-cyclic phosphodiesterase
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