ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Complement decay-accelerating factor

Intramolecular
Cysteine 163 and cysteine 204
Cysteine 253 and cysteine 283
Cysteine 190 and cysteine 220
Cysteine 225 and cysteine 267
Cysteine 36 and cysteine 81
Cysteine 65 and cysteine 94
Cysteine 129 and cysteine 158
Cysteine 98 and cysteine 145
Cysteine 253 and cysteine 254
Cysteine 283 and cysteine 254
A redox-regulated disulphide may form within Complement decay-accelerating factor between cysteines 163 and 204 (131 and 172 respectively in this structure).

Details

Redox score ?
88
PDB code
1ojy
Structure name
decay accelerating factor (cd55): the structure of an intact human complement regulator
Structure deposition date
2003-07-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08174
Residue number A
163
Residue number B
204
Peptide name
Complement decay-accelerating factor

Ligandability

Cysteine 163 of Complement decay-accelerating factor

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 204 of Complement decay-accelerating factor

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 Complement decay-accelerating factor between cysteines 253 and 283 (97 and 127 respectively in this structure).

Details

Redox score ?
88
PDB code
1uot
Structure name
human cd55 domains 3 & 4
Structure deposition date
2003-09-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08174
Residue number A
253
Residue number B
283
Peptide name
Complement decay-accelerating factor

Ligandability

Cysteine 253 of Complement decay-accelerating factor

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 283 of Complement decay-accelerating factor

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 Complement decay-accelerating factor between cysteines 190 and 220.

Details

Redox score ?
88
PDB code
7do4
Structure name
crystal structure of cd97-cd55 complex
Structure deposition date
2020-12-11
Thiol separation (Å)
2
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08174
Residue number A
190
Residue number B
220
Peptide name
Complement decay-accelerating factor

Ligandability

Cysteine 190 of Complement decay-accelerating factor

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 220 of Complement decay-accelerating factor

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 Complement decay-accelerating factor between cysteines 225 and 267 (69 and 111 respectively in this structure).

Details

Redox score ?
87
PDB code
1h04
Structure name
human cd55 domains 3 & 4
Structure deposition date
2002-06-11
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08174
Residue number A
225
Residue number B
267
Peptide name
Complement decay-accelerating factor

Ligandability

Cysteine 225 of Complement decay-accelerating factor

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 267 of Complement decay-accelerating factor

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 Complement decay-accelerating factor between cysteines 36 and 81 (4 and 49 respectively in this structure).

Details

Redox score ?
87
PDB code
1ojy
Structure name
decay accelerating factor (cd55): the structure of an intact human complement regulator
Structure deposition date
2003-07-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08174
Residue number A
36
Residue number B
81
Peptide name
Complement decay-accelerating factor

Ligandability

Cysteine 36 of Complement decay-accelerating factor

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 81 of Complement decay-accelerating factor

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 Complement decay-accelerating factor between cysteines 65 and 94 (33 and 62 respectively in this structure).

Details

Redox score ?
86
PDB code
1ok2
Structure name
decay accelerating factor (cd55): the structure of an intact human complement regulator
Structure deposition date
2003-07-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08174
Residue number A
65
Residue number B
94
Peptide name
Complement decay-accelerating factor

Ligandability

Cysteine 65 of Complement decay-accelerating factor

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 94 of Complement decay-accelerating factor

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 Complement decay-accelerating factor between cysteines 129 and 158 (97 and 126 respectively in this structure).

Details

Redox score ?
85
PDB code
1ojv
Structure name
decay accelerating factor (cd55): the structure of an intact human complement regulator
Structure deposition date
2003-07-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08174
Residue number A
129
Residue number B
158
Peptide name
Complement decay-accelerating factor

Ligandability

Cysteine 129 of Complement decay-accelerating factor

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 158 of Complement decay-accelerating factor

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 Complement decay-accelerating factor between cysteines 98 and 145 (66 and 113 respectively in this structure).

Details

Redox score ?
85
PDB code
1ojy
Structure name
decay accelerating factor (cd55): the structure of an intact human complement regulator
Structure deposition date
2003-07-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08174
Residue number A
98
Residue number B
145
Peptide name
Complement decay-accelerating factor

Ligandability

Cysteine 98 of Complement decay-accelerating factor

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 145 of Complement decay-accelerating factor

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 Complement decay-accelerating factor between cysteines 253 and 254 (221 and 254 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
1ok1
Structure name
decay accelerating factor (cd55): the structure of an intact human complement regulator
Structure deposition date
2003-07-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
nan
Minimum pKa ?
8
% buried
nan
Peptide accession
P08174
Residue number A
253
Residue number B
254
Peptide name
Complement decay-accelerating factor

Ligandability

Cysteine 253 of Complement decay-accelerating factor

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 254 of Complement decay-accelerating factor

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 254 in protein B could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within Complement decay-accelerating factor between cysteines 283 and 254 (251 and 254 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
1ok1
Structure name
decay accelerating factor (cd55): the structure of an intact human complement regulator
Structure deposition date
2003-07-16
Thiol separation (Å)
10
Half-sphere exposure sum ?
nan
Minimum pKa ?
8
% buried
nan
Peptide accession
P08174
Residue number A
283
Residue number B
254
Peptide name
Complement decay-accelerating factor

Ligandability

Cysteine 283 of Complement decay-accelerating factor

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 254 of Complement decay-accelerating factor

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 254 in protein B could not be asigned to a Uniprot residue.
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