ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Properdin

Intermolecular
Cysteine 127 and cysteine 391
Cysteine 455 and cysteine 127
Cysteine 89 and cysteine 391
Intramolecular
Cysteine 205 and cysteine 248
Cysteine 350 and cysteine 360
Cysteine 148 and cysteine 184
Cysteine 224 and cysteine 238
Cysteine 284 and cysteine 296
Cysteine 391 and cysteine 455
Cysteine 407 and cysteine 439
More...
Cysteine 132 and cysteine 170
Cysteine 209 and cysteine 254
Cysteine 163 and cysteine 174
Cysteine 269 and cysteine 306
Cysteine 43 and cysteine 72
Cysteine 104 and cysteine 111
Cysteine 395 and cysteine 461
Cysteine 337 and cysteine 376
Cysteine 93 and cysteine 133
Cysteine 152 and cysteine 190
Cysteine 273 and cysteine 312
Cysteine 89 and cysteine 127
Cysteine 327 and cysteine 370
Cysteine 32 and cysteine 56
Cysteine 57 and cysteine 75
Cysteine 56 and cysteine 75
Cysteine 56 and cysteine 57
Cysteine 132 and cysteine 133
Cysteine 32 and cysteine 75
Cysteine 32 and cysteine 57
Cysteine 89 and cysteine 93
Cysteine 93 and cysteine 170
Cysteine 133 and cysteine 170
Cysteine 93 and cysteine 132
Cysteine 32 and cysteine 43
Cysteine 43 and cysteine 56
Cysteine 43 and cysteine 75
Cysteine 72 and cysteine 75
Cysteine 148 and cysteine 152
Cysteine 56 and cysteine 72
A redox-regulated disulphide may form between two units of Properdin at cysteines 127 and 391. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
7noz
Structure name
structure of the nanobody stablized properdin bound alternative pathway proconvertase c3b:fb:fp
Structure deposition date
2021-02-26
Thiol separation (Å)
9
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide A name
Properdin
Peptide B name
Properdin
Peptide A accession
P27918
Peptide B accession
P27918
Peptide A residue number
127
Peptide B residue number
391

Ligandability

Cysteine 127 of Properdin

Cysteine 391 of Properdin

A redox-regulated disulphide may form between two units of Properdin at cysteines 455 and 127. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
6s0a
Structure name
crystal structure of properdin (tsr domains n12 & 456)
Structure deposition date
2019-06-14
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide A name
Properdin
Peptide B name
Properdin
Peptide A accession
P27918
Peptide B accession
P27918
Peptide A residue number
455
Peptide B residue number
127

Ligandability

Cysteine 455 of Properdin

Cysteine 127 of Properdin

A redox-regulated disulphide may form between two units of Properdin at cysteines 89 and 391. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
6sej
Structure name
structure of a functional monomeric properdin lacking tsr3
Structure deposition date
2019-07-30
Thiol separation (Å)
10
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide A name
Properdin
Peptide B name
Properdin
Peptide A accession
P27918
Peptide B accession
P27918
Peptide A residue number
89
Peptide B residue number
391

Ligandability

Cysteine 89 of Properdin

Cysteine 391 of Properdin

A redox-regulated disulphide may form within Properdin between cysteines 205 and 248.

Details

Redox score ?
89
PDB code
6rus
Structure name
structure of a functional properdin monomer
Structure deposition date
2019-05-29
Thiol separation (Å)
2
Half-sphere exposure sum ?
45
Minimum pKa ?
nan
% buried
nan
Peptide accession
P27918
Residue number A
205
Residue number B
248
Peptide name
Properdin

Ligandability

Cysteine 205 of Properdin

Cysteine 248 of Properdin

A redox-regulated disulphide may form within Properdin between cysteines 350 and 360.

Details

Redox score ?
89
PDB code
6sej
Structure name
structure of a functional monomeric properdin lacking tsr3
Structure deposition date
2019-07-30
Thiol separation (Å)
2
Half-sphere exposure sum ?
44
Minimum pKa ?
nan
% buried
nan
Peptide accession
P27918
Residue number A
350
Residue number B
360
Peptide name
Properdin

Ligandability

Cysteine 350 of Properdin

Cysteine 360 of Properdin

A redox-regulated disulphide may form within Properdin between cysteines 148 and 184.

Details

Redox score ?
88
PDB code
6sej
Structure name
structure of a functional monomeric properdin lacking tsr3
Structure deposition date
2019-07-30
Thiol separation (Å)
2
Half-sphere exposure sum ?
42
Minimum pKa ?
nan
% buried
nan
Peptide accession
P27918
Residue number A
148
Residue number B
184
Peptide name
Properdin

Ligandability

Cysteine 148 of Properdin

Cysteine 184 of Properdin

A redox-regulated disulphide may form within Properdin between cysteines 224 and 238.

Details

Redox score ?
88
PDB code
6rus
Structure name
structure of a functional properdin monomer
Structure deposition date
2019-05-29
Thiol separation (Å)
2
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide accession
P27918
Residue number A
224
Residue number B
238
Peptide name
Properdin

Ligandability

Cysteine 224 of Properdin

Cysteine 238 of Properdin

A redox-regulated disulphide may form within Properdin between cysteines 284 and 296.

Details

Redox score ?
88
PDB code
7noz
Structure name
structure of the nanobody stablized properdin bound alternative pathway proconvertase c3b:fb:fp
Structure deposition date
2021-02-26
Thiol separation (Å)
2
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
P27918
Residue number A
284
Residue number B
296
Peptide name
Properdin

Ligandability

Cysteine 284 of Properdin

Cysteine 296 of Properdin

A redox-regulated disulphide may form within Properdin between cysteines 391 and 455.

Details

Redox score ?
87
PDB code
6rur
Structure name
structure of the scin stabilized c3bbb convertase bound to properdin
Structure deposition date
2019-05-29
Thiol separation (Å)
2
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
P27918
Residue number A
391
Residue number B
455
Peptide name
Properdin

Ligandability

Cysteine 391 of Properdin

Cysteine 455 of Properdin

A redox-regulated disulphide may form within Properdin between cysteines 407 and 439.

Details

Redox score ?
87
PDB code
6sej
Structure name
structure of a functional monomeric properdin lacking tsr3
Structure deposition date
2019-07-30
Thiol separation (Å)
2
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
P27918
Residue number A
407
Residue number B
439
Peptide name
Properdin

Ligandability

Cysteine 407 of Properdin

Cysteine 439 of Properdin

A redox-regulated disulphide may form within Properdin between cysteines 132 and 170.

Details

Redox score ?
87
PDB code
6rus
Structure name
structure of a functional properdin monomer
Structure deposition date
2019-05-29
Thiol separation (Å)
2
Half-sphere exposure sum ?
34
Minimum pKa ?
nan
% buried
nan
Peptide accession
P27918
Residue number A
132
Residue number B
170
Peptide name
Properdin

Ligandability

Cysteine 132 of Properdin

Cysteine 170 of Properdin

A redox-regulated disulphide may form within Properdin between cysteines 209 and 254.

Details

Redox score ?
87
PDB code
6rus
Structure name
structure of a functional properdin monomer
Structure deposition date
2019-05-29
Thiol separation (Å)
2
Half-sphere exposure sum ?
39
Minimum pKa ?
nan
% buried
nan
Peptide accession
P27918
Residue number A
209
Residue number B
254
Peptide name
Properdin

Ligandability

Cysteine 209 of Properdin

Cysteine 254 of Properdin

A redox-regulated disulphide may form within Properdin between cysteines 163 and 174.

Details

Redox score ?
87
PDB code
7noz
Structure name
structure of the nanobody stablized properdin bound alternative pathway proconvertase c3b:fb:fp
Structure deposition date
2021-02-26
Thiol separation (Å)
2
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
P27918
Residue number A
163
Residue number B
174
Peptide name
Properdin

Ligandability

Cysteine 163 of Properdin

Cysteine 174 of Properdin

A redox-regulated disulphide may form within Properdin between cysteines 269 and 306.

Details

Redox score ?
87
PDB code
6sej
Structure name
structure of a functional monomeric properdin lacking tsr3
Structure deposition date
2019-07-30
Thiol separation (Å)
2
Half-sphere exposure sum ?
44
Minimum pKa ?
nan
% buried
nan
Peptide accession
P27918
Residue number A
269
Residue number B
306
Peptide name
Properdin

Ligandability

Cysteine 269 of Properdin

Cysteine 306 of Properdin

A redox-regulated disulphide may form within Properdin between cysteines 43 and 72.

Details

Redox score ?
86
PDB code
6rur
Structure name
structure of the scin stabilized c3bbb convertase bound to properdin
Structure deposition date
2019-05-29
Thiol separation (Å)
2
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
P27918
Residue number A
43
Residue number B
72
Peptide name
Properdin

Ligandability

Cysteine 43 of Properdin

Cysteine 72 of Properdin

A redox-regulated disulphide may form within Properdin between cysteines 104 and 111.

Details

Redox score ?
86
PDB code
7noz
Structure name
structure of the nanobody stablized properdin bound alternative pathway proconvertase c3b:fb:fp
Structure deposition date
2021-02-26
Thiol separation (Å)
2
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P27918
Residue number A
104
Residue number B
111
Peptide name
Properdin

Ligandability

Cysteine 104 of Properdin

Cysteine 111 of Properdin

A redox-regulated disulphide may form within Properdin between cysteines 395 and 461.

Details

Redox score ?
86
PDB code
6rus
Structure name
structure of a functional properdin monomer
Structure deposition date
2019-05-29
Thiol separation (Å)
2
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
P27918
Residue number A
395
Residue number B
461
Peptide name
Properdin

Ligandability

Cysteine 395 of Properdin

Cysteine 461 of Properdin

A redox-regulated disulphide may form within Properdin between cysteines 337 and 376.

Details

Redox score ?
86
PDB code
7noz
Structure name
structure of the nanobody stablized properdin bound alternative pathway proconvertase c3b:fb:fp
Structure deposition date
2021-02-26
Thiol separation (Å)
2
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
P27918
Residue number A
337
Residue number B
376
Peptide name
Properdin

Ligandability

Cysteine 337 of Properdin

Cysteine 376 of Properdin

A redox-regulated disulphide may form within Properdin between cysteines 93 and 133.

Details

Redox score ?
85
PDB code
6rus
Structure name
structure of a functional properdin monomer
Structure deposition date
2019-05-29
Thiol separation (Å)
2
Half-sphere exposure sum ?
39
Minimum pKa ?
nan
% buried
nan
Peptide accession
P27918
Residue number A
93
Residue number B
133
Peptide name
Properdin

Ligandability

Cysteine 93 of Properdin

Cysteine 133 of Properdin

A redox-regulated disulphide may form within Properdin between cysteines 152 and 190.

Details

Redox score ?
85
PDB code
6rus
Structure name
structure of a functional properdin monomer
Structure deposition date
2019-05-29
Thiol separation (Å)
2
Half-sphere exposure sum ?
39
Minimum pKa ?
nan
% buried
nan
Peptide accession
P27918
Residue number A
152
Residue number B
190
Peptide name
Properdin

Ligandability

Cysteine 152 of Properdin

Cysteine 190 of Properdin

A redox-regulated disulphide may form within Properdin between cysteines 273 and 312.

Details

Redox score ?
85
PDB code
7noz
Structure name
structure of the nanobody stablized properdin bound alternative pathway proconvertase c3b:fb:fp
Structure deposition date
2021-02-26
Thiol separation (Å)
2
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P27918
Residue number A
273
Residue number B
312
Peptide name
Properdin

Ligandability

Cysteine 273 of Properdin

Cysteine 312 of Properdin

A redox-regulated disulphide may form within Properdin between cysteines 89 and 127.

Details

Redox score ?
84
PDB code
6rus
Structure name
structure of a functional properdin monomer
Structure deposition date
2019-05-29
Thiol separation (Å)
2
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P27918
Residue number A
89
Residue number B
127
Peptide name
Properdin

Ligandability

Cysteine 89 of Properdin

Cysteine 127 of Properdin

A redox-regulated disulphide may form within Properdin between cysteines 327 and 370.

Details

Redox score ?
82
PDB code
6sej
Structure name
structure of a functional monomeric properdin lacking tsr3
Structure deposition date
2019-07-30
Thiol separation (Å)
2
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P27918
Residue number A
327
Residue number B
370
Peptide name
Properdin

Ligandability

Cysteine 327 of Properdin

Cysteine 370 of Properdin

A redox-regulated disulphide may form within Properdin between cysteines 32 and 56.

Details

Redox score ?
80
PDB code
6rur
Structure name
structure of the scin stabilized c3bbb convertase bound to properdin
Structure deposition date
2019-05-29
Thiol separation (Å)
2
Half-sphere exposure sum ?
90
Minimum pKa ?
nan
% buried
nan
Peptide accession
P27918
Residue number A
32
Residue number B
56
Peptide name
Properdin

Ligandability

Cysteine 32 of Properdin

Cysteine 56 of Properdin

A redox-regulated disulphide may form within Properdin between cysteines 57 and 75.

Details

Redox score ?
80
PDB code
7b26
Structure name
cirpa1 in complex with pseudo-monomeric properdin lacking tsr2-3
Structure deposition date
2020-11-26
Thiol separation (Å)
2
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
P27918
Residue number A
57
Residue number B
75
Peptide name
Properdin

Ligandability

Cysteine 57 of Properdin

Cysteine 75 of Properdin

A redox-regulated disulphide may form within Properdin between cysteines 56 and 75.

Details

Redox score ?
68
PDB code
6ruv
Structure name
structure of the scin stabilized c3bbb convertase bound to properdin and a the non-inhibitory nanobody hfpnb1
Structure deposition date
2019-05-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
83
Minimum pKa ?
nan
% buried
nan
Peptide accession
P27918
Residue number A
56
Residue number B
75
Peptide name
Properdin

Ligandability

Cysteine 56 of Properdin

Cysteine 75 of Properdin

A redox-regulated disulphide may form within Properdin between cysteines 56 and 57.

Details

Redox score ?
65
PDB code
6s0b
Structure name
crystal structure of properdin in complex with the ctc domain of c3/c3b
Structure deposition date
2019-06-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
84
Minimum pKa ?
nan
% buried
nan
Peptide accession
P27918
Residue number A
56
Residue number B
57
Peptide name
Properdin

Ligandability

Cysteine 56 of Properdin

Cysteine 57 of Properdin

A redox-regulated disulphide may form within Properdin between cysteines 132 and 133.

Details

Redox score ?
62
PDB code
6rur
Structure name
structure of the scin stabilized c3bbb convertase bound to properdin
Structure deposition date
2019-05-29
Thiol separation (Å)
7
Half-sphere exposure sum ?
nan
Minimum pKa ?
9
% buried
nan
Peptide accession
P27918
Residue number A
132
Residue number B
133
Peptide name
Properdin

Ligandability

Cysteine 132 of Properdin

Cysteine 133 of Properdin

A redox-regulated disulphide may form within Properdin between cysteines 32 and 75. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
60
PDB code
6s0b
Structure name
crystal structure of properdin in complex with the ctc domain of c3/c3b
Structure deposition date
2019-06-14
Thiol separation (Å)
6
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
P27918
Residue number A
32
Residue number B
75
Peptide name
Properdin

Ligandability

Cysteine 32 of Properdin

Cysteine 75 of Properdin

A redox-regulated disulphide may form within Properdin between cysteines 32 and 57. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
6sej
Structure name
structure of a functional monomeric properdin lacking tsr3
Structure deposition date
2019-07-30
Thiol separation (Å)
7
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
P27918
Residue number A
32
Residue number B
57
Peptide name
Properdin

Ligandability

Cysteine 32 of Properdin

Cysteine 57 of Properdin

A redox-regulated disulphide may form within Properdin between cysteines 89 and 93. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
6s0b
Structure name
crystal structure of properdin in complex with the ctc domain of c3/c3b
Structure deposition date
2019-06-14
Thiol separation (Å)
9
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P27918
Residue number A
89
Residue number B
93
Peptide name
Properdin

Ligandability

Cysteine 89 of Properdin

Cysteine 93 of Properdin

A redox-regulated disulphide may form within Properdin between cysteines 93 and 170. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
6s0a
Structure name
crystal structure of properdin (tsr domains n12 & 456)
Structure deposition date
2019-06-14
Thiol separation (Å)
9
Half-sphere exposure sum ?
37
Minimum pKa ?
nan
% buried
nan
Peptide accession
P27918
Residue number A
93
Residue number B
170
Peptide name
Properdin

Ligandability

Cysteine 93 of Properdin

Cysteine 170 of Properdin

A redox-regulated disulphide may form within Properdin between cysteines 133 and 170. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
6ruv
Structure name
structure of the scin stabilized c3bbb convertase bound to properdin and a the non-inhibitory nanobody hfpnb1
Structure deposition date
2019-05-29
Thiol separation (Å)
9
Half-sphere exposure sum ?
34
Minimum pKa ?
nan
% buried
nan
Peptide accession
P27918
Residue number A
133
Residue number B
170
Peptide name
Properdin

Ligandability

Cysteine 133 of Properdin

Cysteine 170 of Properdin

A redox-regulated disulphide may form within Properdin between cysteines 93 and 132. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
6sej
Structure name
structure of a functional monomeric properdin lacking tsr3
Structure deposition date
2019-07-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
39
Minimum pKa ?
nan
% buried
nan
Peptide accession
P27918
Residue number A
93
Residue number B
132
Peptide name
Properdin

Ligandability

Cysteine 93 of Properdin

Cysteine 132 of Properdin

A redox-regulated disulphide may form within Properdin between cysteines 32 and 43. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
6s0a
Structure name
crystal structure of properdin (tsr domains n12 & 456)
Structure deposition date
2019-06-14
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
P27918
Residue number A
32
Residue number B
43
Peptide name
Properdin

Ligandability

Cysteine 32 of Properdin

Cysteine 43 of Properdin

A redox-regulated disulphide may form within Properdin between cysteines 43 and 56. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
7noz
Structure name
structure of the nanobody stablized properdin bound alternative pathway proconvertase c3b:fb:fp
Structure deposition date
2021-02-26
Thiol separation (Å)
9
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
P27918
Residue number A
43
Residue number B
56
Peptide name
Properdin

Ligandability

Cysteine 43 of Properdin

Cysteine 56 of Properdin

A redox-regulated disulphide may form within Properdin between cysteines 43 and 75. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
6rur
Structure name
structure of the scin stabilized c3bbb convertase bound to properdin
Structure deposition date
2019-05-29
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P27918
Residue number A
43
Residue number B
75
Peptide name
Properdin

Ligandability

Cysteine 43 of Properdin

Cysteine 75 of Properdin

A redox-regulated disulphide may form within Properdin between cysteines 72 and 75. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
6s0b
Structure name
crystal structure of properdin in complex with the ctc domain of c3/c3b
Structure deposition date
2019-06-14
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
P27918
Residue number A
72
Residue number B
75
Peptide name
Properdin

Ligandability

Cysteine 72 of Properdin

Cysteine 75 of Properdin

A redox-regulated disulphide may form within Properdin between cysteines 148 and 152. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
6rv6
Structure name
structure of properdin lacking tsr3 based on anomalous data
Structure deposition date
2019-05-31
Thiol separation (Å)
10
Half-sphere exposure sum ?
38
Minimum pKa ?
nan
% buried
nan
Peptide accession
P27918
Residue number A
148
Residue number B
152
Peptide name
Properdin

Ligandability

Cysteine 148 of Properdin

Cysteine 152 of Properdin

A redox-regulated disulphide may form within Properdin between cysteines 56 and 72. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
6rur
Structure name
structure of the scin stabilized c3bbb convertase bound to properdin
Structure deposition date
2019-05-29
Thiol separation (Å)
10
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
P27918
Residue number A
56
Residue number B
72
Peptide name
Properdin

Ligandability

Cysteine 56 of Properdin

Cysteine 72 of Properdin

If this tool was useful for finding a disulphide, please cite: