cGMP-specific 3',5'-cyclic phosphodiesterase
Intermolecular
Cysteine 677 and cysteine 677
Intramolecular
Cysteine 624 and cysteine 763
Cysteine 367 and cysteine 468
Cysteine 825 and cysteine 846
Cysteine 624 and cysteine 839
Cysteine 191 and cysteine 220
Cysteine 453 and cysteine 468
Cysteine 468 and cysteine 499
Cysteine 169 and cysteine 191
Cysteine 763 and cysteine 839
More...Cysteine 169 and cysteine 310
Cysteine 367 and cysteine 453
Cysteine 367 and cysteine 499
3jwq A 677 B 677
A redox-regulated disulphide may form between two units of cGMP-specific 3',5'-cyclic phosphodiesterase at cysteines 677 and 677.
Details
Redox score ?
79
PDB code
3jwq
Structure name
crystal structure of chimeric pde5/pde6 catalytic domain complexed with sildenafil
Structure deposition date
2009-09-18
Thiol separation (Å)
3
Half-sphere exposure sum ?
48
Minimum pKa ?
9
% buried
29
Peptide A name
cGMP-specific 3',5'-cyclic phosphodiesterase
Peptide B name
cGMP-specific 3',5'-cyclic phosphodiesterase
Peptide A accession
O76074
Peptide B accession
O76074
Peptide A residue number
677
Peptide B residue number
677
Ligandability
2h44 A 624 A 763
A redox-regulated disulphide may form within cGMP-specific 3',5'-cyclic phosphodiesterase between cysteines 624 and 763.
Details
Redox score ?
68
PDB code
2h44
Structure name
crystal structure of pde5a1 in complex with icarisid ii
Structure deposition date
2006-05-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
92
Minimum pKa ?
7
% buried
100
Peptide accession
O76074
Residue number A
624
Residue number B
763
Peptide name
cGMP-specific 3',5'-cyclic phosphodiesterase
Ligandability
Cysteine 624 of cGMP-specific 3',5'-cyclic phosphodiesterase
Cysteine 763 of cGMP-specific 3',5'-cyclic phosphodiesterase
3mf0 B 367 B 468
A redox-regulated disulphide may form within cGMP-specific 3',5'-cyclic phosphodiesterase between cysteines 367 and 468.
Details
Redox score ?
63
PDB code
3mf0
Structure name
crystal structure of pde5a gaf domain (89-518)
Structure deposition date
2010-04-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
92
Minimum pKa ?
8
% buried
100
Peptide accession
O76074
Residue number A
367
Residue number B
468
Peptide name
cGMP-specific 3',5'-cyclic phosphodiesterase
Ligandability
Cysteine 367 of cGMP-specific 3',5'-cyclic phosphodiesterase
Cysteine 468 of cGMP-specific 3',5'-cyclic phosphodiesterase
3jwq A 825 A 846
A redox-regulated disulphide may form within cGMP-specific 3',5'-cyclic phosphodiesterase between cysteines 825 and 846. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
56
PDB code
3jwq
Structure name
crystal structure of chimeric pde5/pde6 catalytic domain complexed with sildenafil
Structure deposition date
2009-09-18
Thiol separation (Å)
5
Half-sphere exposure sum ?
75
Minimum pKa ?
12
% buried
92
Peptide accession
O76074
Residue number A
825
Residue number B
846
Peptide name
cGMP-specific 3',5'-cyclic phosphodiesterase
Ligandability
Cysteine 825 of cGMP-specific 3',5'-cyclic phosphodiesterase
Cysteine 846 of cGMP-specific 3',5'-cyclic phosphodiesterase
2h42 C 624 C 839
A redox-regulated disulphide may form within cGMP-specific 3',5'-cyclic phosphodiesterase between cysteines 624 and 839. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
2h42
Structure name
crystal structure of pde5 in complex with sildenafil
Structure deposition date
2006-05-23
Thiol separation (Å)
8
Half-sphere exposure sum ?
85
Minimum pKa ?
7
% buried
91
Peptide accession
O76074
Residue number A
624
Residue number B
839
Peptide name
cGMP-specific 3',5'-cyclic phosphodiesterase
Ligandability
Cysteine 624 of cGMP-specific 3',5'-cyclic phosphodiesterase
Cysteine 839 of cGMP-specific 3',5'-cyclic phosphodiesterase
3mf0 A 191 A 220
A redox-regulated disulphide may form within cGMP-specific 3',5'-cyclic phosphodiesterase between cysteines 191 and 220. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
3mf0
Structure name
crystal structure of pde5a gaf domain (89-518)
Structure deposition date
2010-04-01
Thiol separation (Å)
8
Half-sphere exposure sum ?
48
Minimum pKa ?
9
% buried
46
Peptide accession
O76074
Residue number A
191
Residue number B
220
Peptide name
cGMP-specific 3',5'-cyclic phosphodiesterase
Ligandability
Cysteine 191 of cGMP-specific 3',5'-cyclic phosphodiesterase
Cysteine 220 of cGMP-specific 3',5'-cyclic phosphodiesterase
3mf0 B 453 B 468
A redox-regulated disulphide may form within cGMP-specific 3',5'-cyclic phosphodiesterase between cysteines 453 and 468. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
3mf0
Structure name
crystal structure of pde5a gaf domain (89-518)
Structure deposition date
2010-04-01
Thiol separation (Å)
7
Half-sphere exposure sum ?
91
Minimum pKa ?
8
% buried
100
Peptide accession
O76074
Residue number A
453
Residue number B
468
Peptide name
cGMP-specific 3',5'-cyclic phosphodiesterase
Ligandability
Cysteine 453 of cGMP-specific 3',5'-cyclic phosphodiesterase
Cysteine 468 of cGMP-specific 3',5'-cyclic phosphodiesterase
3lfv B 468 B 499
A redox-regulated disulphide may form within cGMP-specific 3',5'-cyclic phosphodiesterase between cysteines 468 and 499. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
3lfv
Structure name
crystal structure of unliganded pde5a gaf domain
Structure deposition date
2010-01-18
Thiol separation (Å)
6
Half-sphere exposure sum ?
99
Minimum pKa ?
8
% buried
100
Peptide accession
O76074
Residue number A
468
Residue number B
499
Peptide name
cGMP-specific 3',5'-cyclic phosphodiesterase
Ligandability
Cysteine 468 of cGMP-specific 3',5'-cyclic phosphodiesterase
Cysteine 499 of cGMP-specific 3',5'-cyclic phosphodiesterase
3lfv A 169 A 191
A redox-regulated disulphide may form within cGMP-specific 3',5'-cyclic phosphodiesterase between cysteines 169 and 191. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
3lfv
Structure name
crystal structure of unliganded pde5a gaf domain
Structure deposition date
2010-01-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
11
% buried
84
Peptide accession
O76074
Residue number A
169
Residue number B
191
Peptide name
cGMP-specific 3',5'-cyclic phosphodiesterase
Ligandability
Cysteine 169 of cGMP-specific 3',5'-cyclic phosphodiesterase
Cysteine 191 of cGMP-specific 3',5'-cyclic phosphodiesterase
1udu B 763 B 839
A redox-regulated disulphide may form within cGMP-specific 3',5'-cyclic phosphodiesterase between cysteines 763 and 839. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
1udu
Structure name
crystal structure of human phosphodiesterase 5 complexed with tadalafil(cialis)
Structure deposition date
2003-05-06
Thiol separation (Å)
9
Half-sphere exposure sum ?
81
Minimum pKa ?
12
% buried
88
Peptide accession
O76074
Residue number A
763
Residue number B
839
Peptide name
cGMP-specific 3',5'-cyclic phosphodiesterase
Ligandability
Cysteine 763 of cGMP-specific 3',5'-cyclic phosphodiesterase
Cysteine 839 of cGMP-specific 3',5'-cyclic phosphodiesterase
3lfv B 169 B 310
A redox-regulated disulphide may form within cGMP-specific 3',5'-cyclic phosphodiesterase between cysteines 169 and 310. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
3lfv
Structure name
crystal structure of unliganded pde5a gaf domain
Structure deposition date
2010-01-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
90
Minimum pKa ?
12
% buried
94
Peptide accession
O76074
Residue number A
169
Residue number B
310
Peptide name
cGMP-specific 3',5'-cyclic phosphodiesterase
Ligandability
Cysteine 169 of cGMP-specific 3',5'-cyclic phosphodiesterase
Cysteine 310 of cGMP-specific 3',5'-cyclic phosphodiesterase
3lfv B 367 B 453
A redox-regulated disulphide may form within cGMP-specific 3',5'-cyclic phosphodiesterase between cysteines 367 and 453. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
28
PDB code
3lfv
Structure name
crystal structure of unliganded pde5a gaf domain
Structure deposition date
2010-01-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
84
Minimum pKa ?
13
% buried
100
Peptide accession
O76074
Residue number A
367
Residue number B
453
Peptide name
cGMP-specific 3',5'-cyclic phosphodiesterase
Ligandability
Cysteine 367 of cGMP-specific 3',5'-cyclic phosphodiesterase
Cysteine 453 of cGMP-specific 3',5'-cyclic phosphodiesterase
3lfv B 367 B 499
A redox-regulated disulphide may form within cGMP-specific 3',5'-cyclic phosphodiesterase between cysteines 367 and 499. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
28
PDB code
3lfv
Structure name
crystal structure of unliganded pde5a gaf domain
Structure deposition date
2010-01-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
91
Minimum pKa ?
13
% buried
100
Peptide accession
O76074
Residue number A
367
Residue number B
499
Peptide name
cGMP-specific 3',5'-cyclic phosphodiesterase
Ligandability
Cysteine 367 of cGMP-specific 3',5'-cyclic phosphodiesterase
Cysteine 499 of cGMP-specific 3',5'-cyclic phosphodiesterase
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