Complement C1s subcomponent
Intermolecular
Cysteine 549 and cysteine 425
Intramolecular
Cysteine 65 and cysteine 83
Cysteine 386 and cysteine 421
Cysteine 143 and cysteine 156
Cysteine 234 and cysteine 251
Cysteine 321 and cysteine 354
Cysteine 294 and cysteine 341
Cysteine 158 and cysteine 171
Cysteine 359 and cysteine 403
Cysteine 135 and cysteine 147
More...Cysteine 595 and cysteine 618
Cysteine 175 and cysteine 202
Cysteine 628 and cysteine 659
Cysteine 143 and cysteine 147
Cysteine 135 and cysteine 143
Cysteine 147 and cysteine 156
Cysteine 143 and cysteine 171
Cysteine 156 and cysteine 158
Cysteine 135 and cysteine 156
Cysteine 156 and cysteine 171
Cysteine 143 and cysteine 158
5ubm A 549 B 425
A redox-regulated disulphide may form between two units of Complement C1s subcomponent at cysteines 549 and 425.
Details
Redox score ?
64
PDB code
5ubm
Structure name
crystal structure of human c1s in complex with inhibitor gigastasin
Structure deposition date
2016-12-20
Thiol separation (Å)
5
Half-sphere exposure sum ?
75
Minimum pKa ?
7
% buried
80
Peptide A name
Complement C1s subcomponent
Peptide B name
Complement C1s subcomponent
Peptide A accession
P09871
Peptide B accession
P09871
Peptide A residue number
549
Peptide B residue number
425
Ligandability
Cysteine 549 of Complement C1s subcomponent
Cysteine 425 of Complement C1s subcomponent
4lmf A 50 A 68
A redox-regulated disulphide may form within Complement C1s subcomponent between cysteines 65 and 83 (50 and 68 respectively in this structure).
Details
Redox score ?
88
PDB code
4lmf
Structure name
c1s cub1-egf-cub2
Structure deposition date
2013-07-10
Thiol separation (Å)
2
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
P09871
Residue number A
65
Residue number B
83
Peptide name
Complement C1s subcomponent
Ligandability
Cysteine 65 of Complement C1s subcomponent
Cysteine 83 of Complement C1s subcomponent
4j1y A 386 A 421
A redox-regulated disulphide may form within Complement C1s subcomponent between cysteines 386 and 421.
Details
Redox score ?
87
PDB code
4j1y
Structure name
the x-ray crystal structure of human complement protease c1s zymogen
Structure deposition date
2013-02-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P09871
Residue number A
386
Residue number B
421
Peptide name
Complement C1s subcomponent
Ligandability
Cysteine 386 of Complement C1s subcomponent
Cysteine 421 of Complement C1s subcomponent
1nzi B 128 B 141
A redox-regulated disulphide may form within Complement C1s subcomponent between cysteines 143 and 156 (128 and 141 respectively in this structure).
Details
Redox score ?
87
PDB code
1nzi
Structure name
crystal structure of the cub1-egf interaction domain of complement protease c1s
Structure deposition date
2003-02-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P09871
Residue number A
143
Residue number B
156
Peptide name
Complement C1s subcomponent
Ligandability
Cysteine 143 of Complement C1s subcomponent
Cysteine 156 of Complement C1s subcomponent
6f1c B 219 B 236
A redox-regulated disulphide may form within Complement C1s subcomponent between cysteines 234 and 251 (219 and 236 respectively in this structure).
Details
Redox score ?
86
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
P09871
Residue number A
234
Residue number B
251
Peptide name
Complement C1s subcomponent
Ligandability
Cysteine 234 of Complement C1s subcomponent
Cysteine 251 of Complement C1s subcomponent
4lot A 306 A 339
A redox-regulated disulphide may form within Complement C1s subcomponent between cysteines 321 and 354 (306 and 339 respectively in this structure).
Details
Redox score ?
86
PDB code
4lot
Structure name
c1s cub2-ccp1-ccp2
Structure deposition date
2013-07-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P09871
Residue number A
321
Residue number B
354
Peptide name
Complement C1s subcomponent
Ligandability
Cysteine 321 of Complement C1s subcomponent
Cysteine 354 of Complement C1s subcomponent
5ubm B 294 B 341
A redox-regulated disulphide may form within Complement C1s subcomponent between cysteines 294 and 341.
Details
Redox score ?
86
PDB code
5ubm
Structure name
crystal structure of human c1s in complex with inhibitor gigastasin
Structure deposition date
2016-12-20
Thiol separation (Å)
2
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P09871
Residue number A
294
Residue number B
341
Peptide name
Complement C1s subcomponent
Ligandability
Cysteine 294 of Complement C1s subcomponent
Cysteine 341 of Complement C1s subcomponent
4lor A 143 A 156
A redox-regulated disulphide may form within Complement C1s subcomponent between cysteines 158 and 171 (143 and 156 respectively in this structure).
Details
Redox score ?
85
PDB code
4lor
Structure name
c1s cub1-egf-cub2 in complex with a collagen-like peptide from c1q
Structure deposition date
2013-07-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P09871
Residue number A
158
Residue number B
171
Peptide name
Complement C1s subcomponent
Ligandability
Cysteine 158 of Complement C1s subcomponent
Cysteine 171 of Complement C1s subcomponent
5ubm B 359 B 403
A redox-regulated disulphide may form within Complement C1s subcomponent between cysteines 359 and 403.
Details
Redox score ?
84
PDB code
5ubm
Structure name
crystal structure of human c1s in complex with inhibitor gigastasin
Structure deposition date
2016-12-20
Thiol separation (Å)
2
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P09871
Residue number A
359
Residue number B
403
Peptide name
Complement C1s subcomponent
Ligandability
Cysteine 359 of Complement C1s subcomponent
Cysteine 403 of Complement C1s subcomponent
1nzi B 120 B 132
A redox-regulated disulphide may form within Complement C1s subcomponent between cysteines 135 and 147 (120 and 132 respectively in this structure).
Details
Redox score ?
84
PDB code
1nzi
Structure name
crystal structure of the cub1-egf interaction domain of complement protease c1s
Structure deposition date
2003-02-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P09871
Residue number A
135
Residue number B
147
Peptide name
Complement C1s subcomponent
Ligandability
Cysteine 135 of Complement C1s subcomponent
Cysteine 147 of Complement C1s subcomponent
4j1y B 595 B 618
A redox-regulated disulphide may form within Complement C1s subcomponent between cysteines 595 and 618.
Details
Redox score ?
83
PDB code
4j1y
Structure name
the x-ray crystal structure of human complement protease c1s zymogen
Structure deposition date
2013-02-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
P09871
Residue number A
595
Residue number B
618
Peptide name
Complement C1s subcomponent
Ligandability
Cysteine 595 of Complement C1s subcomponent
Cysteine 618 of Complement C1s subcomponent
6f1c D 160 D 187
A redox-regulated disulphide may form within Complement C1s subcomponent between cysteines 175 and 202 (160 and 187 respectively in this structure).
Details
Redox score ?
81
PDB code
6f1c
Structure name
c1rc1s complex
Structure deposition date
2017-11-21
Thiol separation (Å)
3
Half-sphere exposure sum ?
59
Minimum pKa ?
7
% buried
73
Peptide accession
P09871
Residue number A
175
Residue number B
202
Peptide name
Complement C1s subcomponent
Ligandability
Cysteine 175 of Complement C1s subcomponent
Cysteine 202 of Complement C1s subcomponent
5ubm A 628 A 659
A redox-regulated disulphide may form within Complement C1s subcomponent between cysteines 628 and 659.
Details
Redox score ?
77
PDB code
5ubm
Structure name
crystal structure of human c1s in complex with inhibitor gigastasin
Structure deposition date
2016-12-20
Thiol separation (Å)
2
Half-sphere exposure sum ?
96
Minimum pKa ?
nan
% buried
nan
Peptide accession
P09871
Residue number A
628
Residue number B
659
Peptide name
Complement C1s subcomponent
Ligandability
Cysteine 628 of Complement C1s subcomponent
Cysteine 659 of Complement C1s subcomponent
4lmf B 128 B 132
A redox-regulated disulphide may form within Complement C1s subcomponent between cysteines 143 and 147 (128 and 132 respectively in this structure).
Details
Redox score ?
74
PDB code
4lmf
Structure name
c1s cub1-egf-cub2
Structure deposition date
2013-07-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P09871
Residue number A
143
Residue number B
147
Peptide name
Complement C1s subcomponent
Ligandability
Cysteine 143 of Complement C1s subcomponent
Cysteine 147 of Complement C1s subcomponent
1nzi A 120 A 128
A redox-regulated disulphide may form within Complement C1s subcomponent between cysteines 135 and 143 (120 and 128 respectively in this structure).
Details
Redox score ?
66
PDB code
1nzi
Structure name
crystal structure of the cub1-egf interaction domain of complement protease c1s
Structure deposition date
2003-02-18
Thiol separation (Å)
6
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
P09871
Residue number A
135
Residue number B
143
Peptide name
Complement C1s subcomponent
Ligandability
Cysteine 135 of Complement C1s subcomponent
Cysteine 143 of Complement C1s subcomponent
6f1h D 132 D 141
A redox-regulated disulphide may form within Complement C1s subcomponent between cysteines 147 and 156 (132 and 141 respectively in this structure).
Details
Redox score ?
62
PDB code
6f1h
Structure name
c1rc1s complex
Structure deposition date
2017-11-22
Thiol separation (Å)
6
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P09871
Residue number A
147
Residue number B
156
Peptide name
Complement C1s subcomponent
Ligandability
Cysteine 147 of Complement C1s subcomponent
Cysteine 156 of Complement C1s subcomponent
1nzi B 128 B 156
A redox-regulated disulphide may form within Complement C1s subcomponent between cysteines 143 and 171 (128 and 156 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
1nzi
Structure name
crystal structure of the cub1-egf interaction domain of complement protease c1s
Structure deposition date
2003-02-18
Thiol separation (Å)
8
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
P09871
Residue number A
143
Residue number B
171
Peptide name
Complement C1s subcomponent
Ligandability
Cysteine 143 of Complement C1s subcomponent
Cysteine 171 of Complement C1s subcomponent
4lmf D 141 D 143
A redox-regulated disulphide may form within Complement C1s subcomponent between cysteines 156 and 158 (141 and 143 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
4lmf
Structure name
c1s cub1-egf-cub2
Structure deposition date
2013-07-10
Thiol separation (Å)
8
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
P09871
Residue number A
156
Residue number B
158
Peptide name
Complement C1s subcomponent
Ligandability
Cysteine 156 of Complement C1s subcomponent
Cysteine 158 of Complement C1s subcomponent
1nzi A 120 A 141
A redox-regulated disulphide may form within Complement C1s subcomponent between cysteines 135 and 156 (120 and 141 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
1nzi
Structure name
crystal structure of the cub1-egf interaction domain of complement protease c1s
Structure deposition date
2003-02-18
Thiol separation (Å)
8
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
P09871
Residue number A
135
Residue number B
156
Peptide name
Complement C1s subcomponent
Ligandability
Cysteine 135 of Complement C1s subcomponent
Cysteine 156 of Complement C1s subcomponent
6f1h D 141 D 156
A redox-regulated disulphide may form within Complement C1s subcomponent between cysteines 156 and 171 (141 and 156 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
52
PDB code
6f1h
Structure name
c1rc1s complex
Structure deposition date
2017-11-22
Thiol separation (Å)
8
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P09871
Residue number A
156
Residue number B
171
Peptide name
Complement C1s subcomponent
Ligandability
Cysteine 156 of Complement C1s subcomponent
Cysteine 171 of Complement C1s subcomponent
4lor A 128 A 143
A redox-regulated disulphide may form within Complement C1s subcomponent between cysteines 143 and 158 (128 and 143 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
4lor
Structure name
c1s cub1-egf-cub2 in complex with a collagen-like peptide from c1q
Structure deposition date
2013-07-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
P09871
Residue number A
143
Residue number B
158
Peptide name
Complement C1s subcomponent
Ligandability
Cysteine 143 of Complement C1s subcomponent
Cysteine 158 of Complement C1s subcomponent
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