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a tool for identifying drug-targetable redox-active disulphides

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Complement C1r subcomponent

Intramolecular
Cysteine 406 and cysteine 447
Cysteine 176 and cysteine 189
Cysteine 250 and cysteine 268
Cysteine 161 and cysteine 174
Cysteine 193 and cysteine 220
Cysteine 376 and cysteine 429
Cysteine 338 and cysteine 371
Cysteine 309 and cysteine 358
Cysteine 146 and cysteine 165
Cysteine 71 and cysteine 89
More...
Cysteine 620 and cysteine 639
Cysteine 650 and cysteine 680
Cysteine 451 and cysteine 577
Cysteine 161 and cysteine 189
Cysteine 161 and cysteine 165
Cysteine 165 and cysteine 174
Cysteine 174 and cysteine 189
Cysteine 146 and cysteine 174
Cysteine 146 and cysteine 161
Cysteine 620 and cysteine 680
Cysteine 161 and cysteine 176
Cysteine 174 and cysteine 176
Cysteine 165 and cysteine 176
Cysteine 165 and cysteine 189
Cysteine 639 and cysteine 680
Cysteine 146 and cysteine 176
Cysteine 620 and cysteine 650
Cysteine 146 and cysteine 189
A redox-regulated disulphide may form within Complement C1r subcomponent between cysteines 406 and 447.

Details

Redox score ?
87
PDB code
7mzt
Structure name
borrelia burgdorferi bbk32-c in complex with an autolytic fragment of human c1r at 4
Structure deposition date
2021-05-24
Thiol separation (Å)
2
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00736
Residue number A
406
Residue number B
447
Peptide name
Complement C1r subcomponent

Ligandability

Cysteine 406 of Complement C1r subcomponent

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 447 of Complement C1r subcomponent

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 C1r subcomponent between cysteines 176 and 189 (159 and 172 respectively in this structure).

Details

Redox score ?
87
PDB code
6f1c
Structure name
c1rc1s complex
Structure deposition date
2017-11-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00736
Residue number A
176
Residue number B
189
Peptide name
Complement C1r subcomponent

Ligandability

Cysteine 176 of Complement C1r subcomponent

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 189 of Complement C1r subcomponent

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 C1r subcomponent between cysteines 250 and 268 (233 and 251 respectively in this structure).

Details

Redox score ?
87
PDB code
6f1c
Structure name
c1rc1s complex
Structure deposition date
2017-11-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00736
Residue number A
250
Residue number B
268
Peptide name
Complement C1r subcomponent

Ligandability

Cysteine 250 of Complement C1r subcomponent

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 268 of Complement C1r subcomponent

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 C1r subcomponent between cysteines 161 and 174 (144 and 157 respectively in this structure).

Details

Redox score ?
87
PDB code
6f1h
Structure name
c1rc1s complex
Structure deposition date
2017-11-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00736
Residue number A
161
Residue number B
174
Peptide name
Complement C1r subcomponent

Ligandability

Cysteine 161 of Complement C1r subcomponent

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 174 of Complement C1r subcomponent

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 C1r subcomponent between cysteines 193 and 220 (176 and 203 respectively in this structure).

Details

Redox score ?
87
PDB code
6f1h
Structure name
c1rc1s complex
Structure deposition date
2017-11-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00736
Residue number A
193
Residue number B
220
Peptide name
Complement C1r subcomponent

Ligandability

Cysteine 193 of Complement C1r subcomponent

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 220 of Complement C1r subcomponent

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 C1r subcomponent between cysteines 376 and 429 (359 and 412 respectively in this structure).

Details

Redox score ?
86
PDB code
1md7
Structure name
monomeric structure of the zymogen of complement protease c1r
Structure deposition date
2002-08-07
Thiol separation (Å)
2
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00736
Residue number A
376
Residue number B
429
Peptide name
Complement C1r subcomponent

Ligandability

Cysteine 376 of Complement C1r subcomponent

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 429 of Complement C1r subcomponent

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 C1r subcomponent between cysteines 338 and 371 (321 and 354 respectively in this structure).

Details

Redox score ?
86
PDB code
1gpz
Structure name
the crystal structure of the zymogen catalytic domain of complement protease c1r
Structure deposition date
2001-11-15
Thiol separation (Å)
2
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00736
Residue number A
338
Residue number B
371
Peptide name
Complement C1r subcomponent

Ligandability

Cysteine 338 of Complement C1r subcomponent

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 371 of Complement C1r subcomponent

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 C1r subcomponent between cysteines 309 and 358 (292 and 341 respectively in this structure).

Details

Redox score ?
86
PDB code
1gpz
Structure name
the crystal structure of the zymogen catalytic domain of complement protease c1r
Structure deposition date
2001-11-15
Thiol separation (Å)
2
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00736
Residue number A
309
Residue number B
358
Peptide name
Complement C1r subcomponent

Ligandability

Cysteine 309 of Complement C1r subcomponent

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 358 of Complement C1r subcomponent

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 C1r subcomponent between cysteines 146 and 165 (129 and 148 respectively in this structure).

Details

Redox score ?
86
PDB code
6f39
Structure name
c1r homodimer cub1-egf-cub2
Structure deposition date
2017-11-28
Thiol separation (Å)
2
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00736
Residue number A
146
Residue number B
165
Peptide name
Complement C1r subcomponent

Ligandability

Cysteine 146 of Complement C1r subcomponent

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 165 of Complement C1r subcomponent

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 C1r subcomponent between cysteines 71 and 89 (54 and 72 respectively in this structure).

Details

Redox score ?
85
PDB code
6f1c
Structure name
c1rc1s complex
Structure deposition date
2017-11-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00736
Residue number A
71
Residue number B
89
Peptide name
Complement C1r subcomponent

Ligandability

Cysteine 71 of Complement C1r subcomponent

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 89 of Complement C1r subcomponent

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 C1r subcomponent between cysteines 620 and 639 (603 and 622 respectively in this structure).

Details

Redox score ?
80
PDB code
1md8
Structure name
monomeric structure of the active catalytic domain of complement protease c1r
Structure deposition date
2002-08-07
Thiol separation (Å)
2
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00736
Residue number A
620
Residue number B
639
Peptide name
Complement C1r subcomponent

Ligandability

Cysteine 620 of Complement C1r subcomponent

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 639 of Complement C1r subcomponent

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 C1r subcomponent between cysteines 650 and 680.

Details

Redox score ?
79
PDB code
7mzt
Structure name
borrelia burgdorferi bbk32-c in complex with an autolytic fragment of human c1r at 4
Structure deposition date
2021-05-24
Thiol separation (Å)
2
Half-sphere exposure sum ?
88
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00736
Residue number A
650
Residue number B
680
Peptide name
Complement C1r subcomponent

Ligandability

Cysteine 650 of Complement C1r subcomponent

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 680 of Complement C1r subcomponent

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 C1r subcomponent between cysteines 451 and 577 (434 and 560 respectively in this structure).

Details

Redox score ?
79
PDB code
1md7
Structure name
monomeric structure of the zymogen of complement protease c1r
Structure deposition date
2002-08-07
Thiol separation (Å)
2
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00736
Residue number A
451
Residue number B
577
Peptide name
Complement C1r subcomponent

Ligandability

Cysteine 451 of Complement C1r subcomponent

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 577 of Complement C1r subcomponent

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 C1r subcomponent between cysteines 161 and 189 (144 and 172 respectively in this structure).

Details

Redox score ?
72
PDB code
6f39
Structure name
c1r homodimer cub1-egf-cub2
Structure deposition date
2017-11-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00736
Residue number A
161
Residue number B
189
Peptide name
Complement C1r subcomponent

Ligandability

Cysteine 161 of Complement C1r subcomponent

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 189 of Complement C1r subcomponent

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 C1r subcomponent between cysteines 161 and 165 (144 and 148 respectively in this structure).

Details

Redox score ?
70
PDB code
6f1h
Structure name
c1rc1s complex
Structure deposition date
2017-11-22
Thiol separation (Å)
5
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00736
Residue number A
161
Residue number B
165
Peptide name
Complement C1r subcomponent

Ligandability

Cysteine 161 of Complement C1r subcomponent

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 165 of Complement C1r subcomponent

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 C1r subcomponent between cysteines 165 and 174 (148 and 157 respectively in this structure).

Details

Redox score ?
69
PDB code
6f39
Structure name
c1r homodimer cub1-egf-cub2
Structure deposition date
2017-11-28
Thiol separation (Å)
5
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00736
Residue number A
165
Residue number B
174
Peptide name
Complement C1r subcomponent

Ligandability

Cysteine 165 of Complement C1r subcomponent

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 174 of Complement C1r subcomponent

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 C1r subcomponent between cysteines 174 and 189 (157 and 172 respectively in this structure).

Details

Redox score ?
63
PDB code
6f39
Structure name
c1r homodimer cub1-egf-cub2
Structure deposition date
2017-11-28
Thiol separation (Å)
6
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00736
Residue number A
174
Residue number B
189
Peptide name
Complement C1r subcomponent

Ligandability

Cysteine 174 of Complement C1r subcomponent

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 189 of Complement C1r subcomponent

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 C1r subcomponent between cysteines 146 and 174 (129 and 157 respectively in this structure).

Details

Redox score ?
61
PDB code
6f39
Structure name
c1r homodimer cub1-egf-cub2
Structure deposition date
2017-11-28
Thiol separation (Å)
7
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00736
Residue number A
146
Residue number B
174
Peptide name
Complement C1r subcomponent

Ligandability

Cysteine 146 of Complement C1r subcomponent

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 174 of Complement C1r subcomponent

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 C1r subcomponent between cysteines 146 and 161 (129 and 144 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
6f39
Structure name
c1r homodimer cub1-egf-cub2
Structure deposition date
2017-11-28
Thiol separation (Å)
7
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00736
Residue number A
146
Residue number B
161
Peptide name
Complement C1r subcomponent

Ligandability

Cysteine 146 of Complement C1r subcomponent

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 C1r subcomponent

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 C1r subcomponent between cysteines 620 and 680 (603 and 663 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
1md7
Structure name
monomeric structure of the zymogen of complement protease c1r
Structure deposition date
2002-08-07
Thiol separation (Å)
8
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00736
Residue number A
620
Residue number B
680
Peptide name
Complement C1r subcomponent

Ligandability

Cysteine 620 of Complement C1r subcomponent

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 680 of Complement C1r subcomponent

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 C1r subcomponent between cysteines 161 and 176 (144 and 159 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
6f1h
Structure name
c1rc1s complex
Structure deposition date
2017-11-22
Thiol separation (Å)
8
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00736
Residue number A
161
Residue number B
176
Peptide name
Complement C1r subcomponent

Ligandability

Cysteine 161 of Complement C1r subcomponent

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 176 of Complement C1r subcomponent

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 C1r subcomponent between cysteines 174 and 176 (157 and 159 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
6f1h
Structure name
c1rc1s complex
Structure deposition date
2017-11-22
Thiol separation (Å)
8
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00736
Residue number A
174
Residue number B
176
Peptide name
Complement C1r subcomponent

Ligandability

Cysteine 174 of Complement C1r subcomponent

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 176 of Complement C1r subcomponent

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 C1r subcomponent between cysteines 165 and 176 (148 and 159 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
6f39
Structure name
c1r homodimer cub1-egf-cub2
Structure deposition date
2017-11-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00736
Residue number A
165
Residue number B
176
Peptide name
Complement C1r subcomponent

Ligandability

Cysteine 165 of Complement C1r subcomponent

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 176 of Complement C1r subcomponent

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 C1r subcomponent between cysteines 165 and 189 (148 and 172 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
6f39
Structure name
c1r homodimer cub1-egf-cub2
Structure deposition date
2017-11-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00736
Residue number A
165
Residue number B
189
Peptide name
Complement C1r subcomponent

Ligandability

Cysteine 165 of Complement C1r subcomponent

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 189 of Complement C1r subcomponent

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 C1r subcomponent between cysteines 639 and 680 (622 and 663 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
1md7
Structure name
monomeric structure of the zymogen of complement protease c1r
Structure deposition date
2002-08-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00736
Residue number A
639
Residue number B
680
Peptide name
Complement C1r subcomponent

Ligandability

Cysteine 639 of Complement C1r subcomponent

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 680 of Complement C1r subcomponent

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 C1r subcomponent between cysteines 146 and 176 (29 and 59 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
1apq
Structure name
structure of the egf-like module of human c1r, nmr, 19 structures
Structure deposition date
1997-07-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00736
Residue number A
146
Residue number B
176
Peptide name
Complement C1r subcomponent

Ligandability

Cysteine 146 of Complement C1r subcomponent

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 176 of Complement C1r subcomponent

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 C1r subcomponent between cysteines 620 and 650 (603 and 633 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
1md7
Structure name
monomeric structure of the zymogen of complement protease c1r
Structure deposition date
2002-08-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00736
Residue number A
620
Residue number B
650
Peptide name
Complement C1r subcomponent

Ligandability

Cysteine 620 of Complement C1r subcomponent

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 650 of Complement C1r subcomponent

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 C1r subcomponent between cysteines 146 and 189 (29 and 72 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
1apq
Structure name
structure of the egf-like module of human c1r, nmr, 19 structures
Structure deposition date
1997-07-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00736
Residue number A
146
Residue number B
189
Peptide name
Complement C1r subcomponent

Ligandability

Cysteine 146 of Complement C1r subcomponent

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 189 of Complement C1r subcomponent

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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