ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Complement factor H-related protein 1

Intramolecular
Cysteine 300 and cysteine 327
Cysteine 266 and cysteine 317
Cysteine 208 and cysteine 251
Cysteine 237 and cysteine 262
A redox-regulated disulphide may form within Complement factor H-related protein 1 between cysteines 300 and 327.

Details

Redox score ?
89
PDB code
4muc
Structure name
the 4th and 5th c-terminal domains of factor h related protein 1
Structure deposition date
2013-09-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q03591
Residue number A
300
Residue number B
327
Peptide name
Complement factor H-related protein 1

Ligandability

Cysteine 300 of Complement factor H-related protein 1

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 327 of Complement factor H-related protein 1

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 H-related protein 1 between cysteines 266 and 317.

Details

Redox score ?
86
PDB code
4muc
Structure name
the 4th and 5th c-terminal domains of factor h related protein 1
Structure deposition date
2013-09-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q03591
Residue number A
266
Residue number B
317
Peptide name
Complement factor H-related protein 1

Ligandability

Cysteine 266 of Complement factor H-related protein 1

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 317 of Complement factor H-related protein 1

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 H-related protein 1 between cysteines 208 and 251 (1109 and 1152 respectively in this structure).

Details

Redox score ?
86
PDB code
3rj3
Structure name
complement components factor h ccp19-20 (s1191l mutant) and c3d in complex
Structure deposition date
2011-04-15
Thiol separation (Å)
2
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q03591
Residue number A
208
Residue number B
251
Peptide name
Complement factor H-related protein 1

Ligandability

Cysteine 208 of Complement factor H-related protein 1

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 251 of Complement factor H-related protein 1

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 H-related protein 1 between cysteines 237 and 262 (1138 and 1163 respectively in this structure).

Details

Redox score ?
83
PDB code
3rj3
Structure name
complement components factor h ccp19-20 (s1191l mutant) and c3d in complex
Structure deposition date
2011-04-15
Thiol separation (Å)
2
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q03591
Residue number A
237
Residue number B
262
Peptide name
Complement factor H-related protein 1

Ligandability

Cysteine 237 of Complement factor H-related protein 1

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 262 of Complement factor H-related protein 1

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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