ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Complement factor D

Intramolecular
Cysteine 155 and cysteine 221
Cysteine 211 and cysteine 236
Cysteine 58 and cysteine 74
Cysteine 186 and cysteine 202
A redox-regulated disulphide may form within Complement factor D between cysteines 155 and 221 (136 and 201 respectively in this structure).

Details

Redox score ?
85
PDB code
4d9q
Structure name
inhibiting alternative pathway complement activation by targeting the exosite on factor d
Structure deposition date
2012-01-11
Thiol separation (Å)
2
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
F6YBP7
Residue number A
155
Residue number B
221
Peptide name
Complement factor D

Ligandability

Cysteine 155 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 221 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 211 and 236 (191 and 220 respectively in this structure).

Details

Redox score ?
81
PDB code
4d9q
Structure name
inhibiting alternative pathway complement activation by targeting the exosite on factor d
Structure deposition date
2012-01-11
Thiol separation (Å)
2
Half-sphere exposure sum ?
86
Minimum pKa ?
nan
% buried
nan
Peptide accession
F6YBP7
Residue number A
211
Residue number B
236
Peptide name
Complement factor D

Ligandability

Cysteine 211 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 236 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 58 and 74 (42 and 58 respectively in this structure).

Details

Redox score ?
79
PDB code
4d9q
Structure name
inhibiting alternative pathway complement activation by targeting the exosite on factor d
Structure deposition date
2012-01-11
Thiol separation (Å)
2
Half-sphere exposure sum ?
91
Minimum pKa ?
nan
% buried
nan
Peptide accession
F6YBP7
Residue number A
58
Residue number B
74
Peptide name
Complement factor D

Ligandability

Cysteine 58 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 74 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 186 and 202 (168 and 182 respectively in this structure).

Details

Redox score ?
78
PDB code
4d9q
Structure name
inhibiting alternative pathway complement activation by targeting the exosite on factor d
Structure deposition date
2012-01-11
Thiol separation (Å)
2
Half-sphere exposure sum ?
90
Minimum pKa ?
nan
% buried
nan
Peptide accession
F6YBP7
Residue number A
186
Residue number B
202
Peptide name
Complement factor D

Ligandability

Cysteine 186 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 202 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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