ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Complement factor D

Intramolecular
Cysteine 148 and cysteine 214
Cysteine 51 and cysteine 67
Cysteine 204 and cysteine 229
Cysteine 179 and cysteine 195
Cysteine 179 and cysteine 229
Cysteine 195 and cysteine 229
Cysteine 195 and cysteine 204
A redox-regulated disulphide may form within Complement factor D between cysteines 148 and 214 (138 and 204 respectively in this structure).

Details

Redox score ?
85
PDB code
5tca
Structure name
complement factor d inhibited with jh3
Structure deposition date
2016-09-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00746
Residue number A
148
Residue number B
214
Peptide name
Complement factor D

Ligandability

Cysteine 148 of Complement factor D

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 214 of Complement factor D

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 factor D between cysteines 51 and 67 (42 and 58 respectively in this structure).

Details

Redox score ?
80
PDB code
6qmt
Structure name
complement factor d in complex with the inhibitor 2-(2-(3'- (aminomethyl)-[1,1'-biphenyl]-3-carboxamido)phenyl)acetic acid
Structure deposition date
2019-02-08
Thiol separation (Å)
2
Half-sphere exposure sum ?
87
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00746
Residue number A
51
Residue number B
67
Peptide name
Complement factor D

Ligandability

Cysteine 51 of Complement factor D

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 67 of Complement factor D

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 factor D between cysteines 204 and 229 (191 and 220 respectively in this structure).

Details

Redox score ?
80
PDB code
1dfp
Structure name
factor d inhibited by diisopropyl fluorophosphate
Structure deposition date
1997-02-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00746
Residue number A
204
Residue number B
229
Peptide name
Complement factor D

Ligandability

Cysteine 204 of Complement factor D

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 229 of Complement factor D

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 factor D between cysteines 179 and 195 (168 and 182 respectively in this structure).

Details

Redox score ?
78
PDB code
6vmk
Structure name
crystal structure of human complement factor d with anti-factor d fab 20d12
Structure deposition date
2020-01-28
Thiol separation (Å)
2
Half-sphere exposure sum ?
90
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00746
Residue number A
179
Residue number B
195
Peptide name
Complement factor D

Ligandability

Cysteine 179 of Complement factor D

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 195 of Complement factor D

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 factor D between cysteines 179 and 229 (154 and 204 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
4cbo
Structure name
crystal structure of complement factor d mutant r202a after ensemble refinement
Structure deposition date
2013-10-15
Thiol separation (Å)
10
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00746
Residue number A
179
Residue number B
229
Peptide name
Complement factor D

Ligandability

Cysteine 179 of Complement factor D

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 229 of Complement factor D

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 factor D between cysteines 195 and 229 (170 and 204 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
4cbo
Structure name
crystal structure of complement factor d mutant r202a after ensemble refinement
Structure deposition date
2013-10-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00746
Residue number A
195
Residue number B
229
Peptide name
Complement factor D

Ligandability

Cysteine 195 of Complement factor D

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 229 of Complement factor D

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 factor D between cysteines 195 and 204 (170 and 179 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
4cbo
Structure name
crystal structure of complement factor d mutant r202a after ensemble refinement
Structure deposition date
2013-10-15
Thiol separation (Å)
10
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00746
Residue number A
195
Residue number B
204
Peptide name
Complement factor D

Ligandability

Cysteine 195 of Complement factor D

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 factor D

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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