ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Complement component C1q receptor

Intramolecular
Cysteine 225 and cysteine 652
Cysteine 188 and cysteine 240
Cysteine 104 and cysteine 136
Cysteine 141 and cysteine 165
Cysteine 31 and cysteine 36
Cysteine 53 and cysteine 180
A redox-regulated disulphide may form within Complement component C1q receptor between cysteines 225 and 652 (225 and 257 respectively in this structure).

Details

Redox score ?
94
PDB code
8a59
Structure name
c-type lectin-like domain (ctld) and sushi-like domain of human cd93
Structure deposition date
2022-06-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NPY3
Residue number A
225
Residue number B
652
Peptide name
Complement component C1q receptor

Ligandability

Cysteine 225 of Complement component C1q receptor

Cysteine 652 of Complement component C1q receptor

A redox-regulated disulphide may form within Complement component C1q receptor between cysteines 188 and 240.

Details

Redox score ?
85
PDB code
8a59
Structure name
c-type lectin-like domain (ctld) and sushi-like domain of human cd93
Structure deposition date
2022-06-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NPY3
Residue number A
188
Residue number B
240
Peptide name
Complement component C1q receptor

Ligandability

Cysteine 188 of Complement component C1q receptor

Cysteine 240 of Complement component C1q receptor

A redox-regulated disulphide may form within Complement component C1q receptor between cysteines 104 and 136.

Details

Redox score ?
84
PDB code
8a59
Structure name
c-type lectin-like domain (ctld) and sushi-like domain of human cd93
Structure deposition date
2022-06-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
40
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NPY3
Residue number A
104
Residue number B
136
Peptide name
Complement component C1q receptor

Ligandability

Cysteine 104 of Complement component C1q receptor

Cysteine 136 of Complement component C1q receptor

A redox-regulated disulphide may form within Complement component C1q receptor between cysteines 141 and 165.

Details

Redox score ?
83
PDB code
8a59
Structure name
c-type lectin-like domain (ctld) and sushi-like domain of human cd93
Structure deposition date
2022-06-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NPY3
Residue number A
141
Residue number B
165
Peptide name
Complement component C1q receptor

Ligandability

Cysteine 141 of Complement component C1q receptor

Cysteine 165 of Complement component C1q receptor

A redox-regulated disulphide may form within Complement component C1q receptor between cysteines 31 and 36.

Details

Redox score ?
81
PDB code
8a59
Structure name
c-type lectin-like domain (ctld) and sushi-like domain of human cd93
Structure deposition date
2022-06-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NPY3
Residue number A
31
Residue number B
36
Peptide name
Complement component C1q receptor

Ligandability

Cysteine 31 of Complement component C1q receptor

Cysteine 36 of Complement component C1q receptor

A redox-regulated disulphide may form within Complement component C1q receptor between cysteines 53 and 180.

Details

Redox score ?
81
PDB code
8a59
Structure name
c-type lectin-like domain (ctld) and sushi-like domain of human cd93
Structure deposition date
2022-06-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NPY3
Residue number A
53
Residue number B
180
Peptide name
Complement component C1q receptor

Ligandability

Cysteine 53 of Complement component C1q receptor

Cysteine 180 of Complement component C1q receptor

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