ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Complement receptor type 1

Intramolecular
Cysteine 104 and cysteine 145
Cysteine 493 and cysteine 536
Cysteine 131 and cysteine 161
Cysteine 73 and cysteine 99
Cysteine 1095 and cysteine 232
Cysteine 43 and cysteine 86
Cysteine 195 and cysteine 232
Cysteine 581 and cysteine 611
Cysteine 523 and cysteine 549
Cysteine 166 and cysteine 215
More...
Cysteine 616 and cysteine 215
Cysteine 554 and cysteine 595
A redox-regulated disulphide may form within Complement receptor type 1 between cysteines 104 and 145 (63 and 104 respectively in this structure).

Details

Redox score ?
89
PDB code
2mcy
Structure name
cr1 sushi domains 2 and 3
Structure deposition date
2013-08-27
Thiol separation (Å)
2
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17927
Residue number A
104
Residue number B
145
Peptide name
Complement receptor type 1

Ligandability

Cysteine 104 of Complement receptor type 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 145 of Complement receptor type 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 receptor type 1 between cysteines 493 and 536 (943 and 986 respectively in this structure).

Details

Redox score ?
88
PDB code
5fo9
Structure name
crystal structure of human complement c3b in complex with cr1 (ccp15- 17)
Structure deposition date
2015-11-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17927
Residue number A
493
Residue number B
536
Peptide name
Complement receptor type 1

Ligandability

Cysteine 493 of Complement receptor type 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 536 of Complement receptor type 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 receptor type 1 between cysteines 131 and 161 (90 and 120 respectively in this structure).

Details

Redox score ?
88
PDB code
2mcy
Structure name
cr1 sushi domains 2 and 3
Structure deposition date
2013-08-27
Thiol separation (Å)
2
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17927
Residue number A
131
Residue number B
161
Peptide name
Complement receptor type 1

Ligandability

Cysteine 131 of Complement receptor type 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 161 of Complement receptor type 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 receptor type 1 between cysteines 73 and 99 (32 and 58 respectively in this structure).

Details

Redox score ?
88
PDB code
2mcz
Structure name
cr1 sushi domains 1 and 2
Structure deposition date
2013-08-27
Thiol separation (Å)
2
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17927
Residue number A
73
Residue number B
99
Peptide name
Complement receptor type 1

Ligandability

Cysteine 73 of Complement receptor type 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 99 of Complement receptor type 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 receptor type 1 between cysteines 1095 and 232 (1095 and 1132 respectively in this structure).

Details

Redox score ?
88
PDB code
5fo9
Structure name
crystal structure of human complement c3b in complex with cr1 (ccp15- 17)
Structure deposition date
2015-11-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17927
Residue number A
1095
Residue number B
232
Peptide name
Complement receptor type 1

Ligandability

Cysteine 1095 of Complement receptor type 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 232 of Complement receptor type 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 receptor type 1 between cysteines 43 and 86 (2 and 45 respectively in this structure).

Details

Redox score ?
88
PDB code
2mcz
Structure name
cr1 sushi domains 1 and 2
Structure deposition date
2013-08-27
Thiol separation (Å)
2
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17927
Residue number A
43
Residue number B
86
Peptide name
Complement receptor type 1

Ligandability

Cysteine 43 of Complement receptor type 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 86 of Complement receptor type 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 receptor type 1 between cysteines 195 and 232 (154 and 191 respectively in this structure).

Details

Redox score ?
87
PDB code
2mcy
Structure name
cr1 sushi domains 2 and 3
Structure deposition date
2013-08-27
Thiol separation (Å)
2
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17927
Residue number A
195
Residue number B
232
Peptide name
Complement receptor type 1

Ligandability

Cysteine 195 of Complement receptor type 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 232 of Complement receptor type 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 receptor type 1 between cysteines 581 and 611 (1031 and 1061 respectively in this structure).

Details

Redox score ?
87
PDB code
5fo9
Structure name
crystal structure of human complement c3b in complex with cr1 (ccp15- 17)
Structure deposition date
2015-11-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17927
Residue number A
581
Residue number B
611
Peptide name
Complement receptor type 1

Ligandability

Cysteine 581 of Complement receptor type 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 611 of Complement receptor type 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 receptor type 1 between cysteines 523 and 549 (973 and 999 respectively in this structure).

Details

Redox score ?
86
PDB code
5fo9
Structure name
crystal structure of human complement c3b in complex with cr1 (ccp15- 17)
Structure deposition date
2015-11-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17927
Residue number A
523
Residue number B
549
Peptide name
Complement receptor type 1

Ligandability

Cysteine 523 of Complement receptor type 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 549 of Complement receptor type 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 receptor type 1 between cysteines 166 and 215 (125 and 174 respectively in this structure).

Details

Redox score ?
85
PDB code
2mcy
Structure name
cr1 sushi domains 2 and 3
Structure deposition date
2013-08-27
Thiol separation (Å)
2
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17927
Residue number A
166
Residue number B
215
Peptide name
Complement receptor type 1

Ligandability

Cysteine 166 of Complement receptor type 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 215 of Complement receptor type 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 receptor type 1 between cysteines 616 and 215 (1066 and 1115 respectively in this structure).

Details

Redox score ?
85
PDB code
5fo9
Structure name
crystal structure of human complement c3b in complex with cr1 (ccp15- 17)
Structure deposition date
2015-11-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17927
Residue number A
616
Residue number B
215
Peptide name
Complement receptor type 1

Ligandability

Cysteine 616 of Complement receptor type 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 215 of Complement receptor type 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 receptor type 1 between cysteines 554 and 595 (1004 and 1045 respectively in this structure).

Details

Redox score ?
84
PDB code
5fo9
Structure name
crystal structure of human complement c3b in complex with cr1 (ccp15- 17)
Structure deposition date
2015-11-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17927
Residue number A
554
Residue number B
595
Peptide name
Complement receptor type 1

Ligandability

Cysteine 554 of Complement receptor type 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 595 of Complement receptor type 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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