ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Complement C3

Intermolecular
Cysteine 559 and cysteine 816
Cysteine 1010 and cysteine 1010
Intramolecular
Cysteine 1637 and cysteine 1646
Cysteine 1506 and cysteine 1511
Cysteine 1535 and cysteine 1659
Cysteine 707 and cysteine 728
Cysteine 1358 and cysteine 1489
Cysteine 1101 and cysteine 1158
Cysteine 693 and cysteine 720
Cysteine 694 and cysteine 727
More...
Cysteine 557 and cysteine 815
Cysteine 627 and cysteine 662
Cysteine 1389 and cysteine 1458
Cysteine 873 and cysteine 1513
Cysteine 1518 and cysteine 1590
Cysteine 1506 and cysteine 1518
Cysteine 693 and cysteine 694
Cysteine 873 and cysteine 1506
Cysteine 727 and cysteine 728
Cysteine 693 and cysteine 727
Cysteine 694 and cysteine 728
Cysteine 1511 and cysteine 1513
Cysteine 1511 and cysteine 1518
Cysteine 707 and cysteine 727
Cysteine 694 and cysteine 720
Cysteine 1506 and cysteine 1513
Cysteine 720 and cysteine 727
Cysteine 1513 and cysteine 1518
Cysteine 1511 and cysteine 1590
Cysteine 873 and cysteine 1511
Cysteine 873 and cysteine 1518
A redox-regulated disulphide may form between two units of Complement C3 at cysteines 559 and 816.

Details

Redox score ?
81
PDB code
5foa
Structure name
crystal structure of human complement c3b in complex with daf (ccp2-4)
Structure deposition date
2015-11-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide A name
Complement C3
Peptide B name
Complement C3
Peptide A accession
P01024
Peptide B accession
P01024
Peptide A residue number
559
Peptide B residue number
816

Ligandability

Cysteine 559 of Complement C3

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 816 of Complement C3

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 between two units of Complement C3 at cysteines 1010 and 1010 (17 and 17 respectively in this structure).

Details

Redox score ?
74
PDB code
6rmu
Structure name
crystal structure of disulphide-linked human c3d dimer in complex with staphylococcus aureus complement subversion protein sbi-iv
Structure deposition date
2019-05-07
Thiol separation (Å)
3
Half-sphere exposure sum ?
92
Minimum pKa ?
nan
% buried
nan
Peptide A name
Complement C3
Peptide B name
Complement C3
Peptide A accession
P01024
Peptide B accession
P01024
Peptide A residue number
1010
Peptide B residue number
1010

Ligandability

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 C3 between cysteines 1637 and 1646 (1615 and 1624 respectively in this structure).

Details

Redox score ?
87
PDB code
2ice
Structure name
crig bound to c3c
Structure deposition date
2006-09-12
Thiol separation (Å)
2
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01024
Residue number A
1637
Residue number B
1646
Peptide name
Complement C3

Ligandability

Cysteine 1637 of Complement C3

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 1646 of Complement C3

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 C3 between cysteines 1506 and 1511.

Details

Redox score ?
87
PDB code
6ehg
Structure name
complement component c3b in complex with a nanobody
Structure deposition date
2017-09-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01024
Residue number A
1506
Residue number B
1511
Peptide name
Complement C3

Ligandability

Cysteine 1506 of Complement C3

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 1511 of Complement C3

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 C3 between cysteines 1535 and 1659.

Details

Redox score ?
87
PDB code
2b39
Structure name
structure of mammalian c3 with an intact thioester at 3a resolution
Structure deposition date
2005-09-20
Thiol separation (Å)
2
Half-sphere exposure sum ?
46
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q2UVX4
Residue number A
1535
Residue number B
1659
Peptide name
Complement C3

Ligandability

Cysteine 1535 of Complement C3

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 1659 of Complement C3

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 C3 between cysteines 707 and 728.

Details

Redox score ?
85
PDB code
4hwj
Structure name
crystal structure of the human c3a desarg anaphylatoxin
Structure deposition date
2012-11-08
Thiol separation (Å)
2
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01024
Residue number A
707
Residue number B
728
Peptide name
Complement C3

Ligandability

Cysteine 707 of Complement C3

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 728 of Complement C3

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 C3 between cysteines 1358 and 1489 (1336 and 1467 respectively in this structure).

Details

Redox score ?
85
PDB code
3g6j
Structure name
c3b in complex with a c3b specific fab
Structure deposition date
2009-02-06
Thiol separation (Å)
2
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01024
Residue number A
1358
Residue number B
1489
Peptide name
Complement C3

Ligandability

Cysteine 1358 of Complement C3

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 1489 of Complement C3

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 C3 between cysteines 1101 and 1158 (1079 and 1136 respectively in this structure).

Details

Redox score ?
85
PDB code
3g6j
Structure name
c3b in complex with a c3b specific fab
Structure deposition date
2009-02-06
Thiol separation (Å)
2
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01024
Residue number A
1101
Residue number B
1158
Peptide name
Complement C3

Ligandability

Cysteine 1101 of Complement C3

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 1158 of Complement C3

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 C3 between cysteines 693 and 720.

Details

Redox score ?
84
PDB code
6ru5
Structure name
human complement c3 in complex with the hc3nb1 nanobody
Structure deposition date
2019-05-27
Thiol separation (Å)
2
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01024
Residue number A
693
Residue number B
720
Peptide name
Complement C3

Ligandability

Cysteine 693 of Complement C3

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 720 of Complement C3

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 C3 between cysteines 694 and 727 (672 and 705 respectively in this structure).

Details

Redox score ?
81
PDB code
2a73
Structure name
human complement component c3
Structure deposition date
2005-07-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01024
Residue number A
694
Residue number B
727
Peptide name
Complement C3

Ligandability

Cysteine 694 of Complement C3

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 727 of Complement C3

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 C3 between cysteines 557 and 815.

Details

Redox score ?
81
PDB code
2b39
Structure name
structure of mammalian c3 with an intact thioester at 3a resolution
Structure deposition date
2005-09-20
Thiol separation (Å)
2
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q2UVX4
Residue number A
557
Residue number B
815
Peptide name
Complement C3

Ligandability

Cysteine 557 of Complement C3

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 815 of Complement C3

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 C3 between cysteines 627 and 662 (605 and 640 respectively in this structure).

Details

Redox score ?
81
PDB code
6ruv
Structure name
structure of the scin stabilized c3bbb convertase bound to properdin and a the non-inhibitory nanobody hfpnb1
Structure deposition date
2019-05-29
Thiol separation (Å)
2
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01024
Residue number A
627
Residue number B
662
Peptide name
Complement C3

Ligandability

Cysteine 627 of Complement C3

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 662 of Complement C3

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 C3 between cysteines 1389 and 1458 (1367 and 1436 respectively in this structure).

Details

Redox score ?
79
PDB code
2wii
Structure name
complement c3b in complex with factor h domains 1-4
Structure deposition date
2009-05-12
Thiol separation (Å)
3
Half-sphere exposure sum ?
48
Minimum pKa ?
9
% buried
12
Peptide accession
P01024
Residue number A
1389
Residue number B
1458
Peptide name
Complement C3

Ligandability

Cysteine 1389 of Complement C3

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 1458 of Complement C3

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 C3 between cysteines 873 and 1513.

Details

Redox score ?
77
PDB code
5o35
Structure name
structure of complement proteins complex
Structure deposition date
2017-05-23
Thiol separation (Å)
3
Half-sphere exposure sum ?
72
Minimum pKa ?
8
% buried
86
Peptide accession
P01024
Residue number A
873
Residue number B
1513
Peptide name
Complement C3

Ligandability

Cysteine 873 of Complement C3

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 1513 of Complement C3

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 C3 between cysteines 1518 and 1590 (1496 and 1568 respectively in this structure).

Details

Redox score ?
73
PDB code
3l5n
Structure name
staphylococcal complement inhibitor (scin) in complex with human complement component c3b
Structure deposition date
2009-12-22
Thiol separation (Å)
5
Half-sphere exposure sum ?
44
Minimum pKa ?
9
% buried
16
Peptide accession
P01024
Residue number A
1518
Residue number B
1590
Peptide name
Complement C3

Ligandability

Cysteine 1518 of Complement C3

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 1590 of Complement C3

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 C3 between cysteines 1506 and 1518. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
5fo8
Structure name
crystal structure of human complement c3b in complex with mcp (ccp1-4)
Structure deposition date
2015-11-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01024
Residue number A
1506
Residue number B
1518
Peptide name
Complement C3

Ligandability

Cysteine 1506 of Complement C3

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 1518 of Complement C3

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 C3 between cysteines 693 and 694 (22 and 23 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
4i6o
Structure name
crystal structure of chemically synthesized human anaphylatoxin c3a
Structure deposition date
2012-11-29
Thiol separation (Å)
9
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01024
Residue number A
693
Residue number B
694
Peptide name
Complement C3

Ligandability

Cysteine 693 of Complement C3

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 694 of Complement C3

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 C3 between cysteines 873 and 1506 (851 and 1484 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
3g6j
Structure name
c3b in complex with a c3b specific fab
Structure deposition date
2009-02-06
Thiol separation (Å)
9
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01024
Residue number A
873
Residue number B
1506
Peptide name
Complement C3

Ligandability

Cysteine 873 of Complement C3

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 1506 of Complement C3

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 C3 between cysteines 727 and 728 (56 and 57 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
4i6o
Structure name
crystal structure of chemically synthesized human anaphylatoxin c3a
Structure deposition date
2012-11-29
Thiol separation (Å)
9
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01024
Residue number A
727
Residue number B
728
Peptide name
Complement C3

Ligandability

Cysteine 727 of Complement C3

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 728 of Complement C3

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 C3 between cysteines 693 and 727. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
4hwj
Structure name
crystal structure of the human c3a desarg anaphylatoxin
Structure deposition date
2012-11-08
Thiol separation (Å)
9
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01024
Residue number A
693
Residue number B
727
Peptide name
Complement C3

Ligandability

Cysteine 693 of Complement C3

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 727 of Complement C3

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 C3 between cysteines 694 and 728 (672 and 706 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
2a73
Structure name
human complement component c3
Structure deposition date
2005-07-04
Thiol separation (Å)
9
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01024
Residue number A
694
Residue number B
728
Peptide name
Complement C3

Ligandability

Cysteine 694 of Complement C3

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 728 of Complement C3

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 C3 between cysteines 1511 and 1513 (1489 and 1491 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
2a74
Structure name
human complement component c3c
Structure deposition date
2005-07-04
Thiol separation (Å)
10
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01024
Residue number A
1511
Residue number B
1513
Peptide name
Complement C3

Ligandability

Cysteine 1511 of Complement C3

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 1513 of Complement C3

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 C3 between cysteines 1511 and 1518 (1489 and 1496 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
2wii
Structure name
complement c3b in complex with factor h domains 1-4
Structure deposition date
2009-05-12
Thiol separation (Å)
9
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01024
Residue number A
1511
Residue number B
1518
Peptide name
Complement C3

Ligandability

Cysteine 1511 of Complement C3

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 1518 of Complement C3

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 C3 between cysteines 707 and 727 (36 and 56 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
4i6o
Structure name
crystal structure of chemically synthesized human anaphylatoxin c3a
Structure deposition date
2012-11-29
Thiol separation (Å)
10
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01024
Residue number A
707
Residue number B
727
Peptide name
Complement C3

Ligandability

Cysteine 707 of Complement C3

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 727 of Complement C3

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 C3 between cysteines 694 and 720. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
4hwj
Structure name
crystal structure of the human c3a desarg anaphylatoxin
Structure deposition date
2012-11-08
Thiol separation (Å)
10
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01024
Residue number A
694
Residue number B
720
Peptide name
Complement C3

Ligandability

Cysteine 694 of Complement C3

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 720 of Complement C3

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 C3 between cysteines 1506 and 1513 (1484 and 1491 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
3l3o
Structure name
staphylococcal complement inhibitor (scin) in complex with human complement component c3c
Structure deposition date
2009-12-17
Thiol separation (Å)
10
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01024
Residue number A
1506
Residue number B
1513
Peptide name
Complement C3

Ligandability

Cysteine 1506 of Complement C3

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 1513 of Complement C3

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 C3 between cysteines 720 and 727. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
4hw5
Structure name
crystal structure of the human c3a anaphylatoxin
Structure deposition date
2012-11-07
Thiol separation (Å)
10
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01024
Residue number A
720
Residue number B
727
Peptide name
Complement C3

Ligandability

Cysteine 720 of Complement C3

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 727 of Complement C3

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 C3 between cysteines 1513 and 1518 (1491 and 1496 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
7bag
Structure name
c3b in complex with cp40
Structure deposition date
2020-12-15
Thiol separation (Å)
10
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01024
Residue number A
1513
Residue number B
1518
Peptide name
Complement C3

Ligandability

Cysteine 1513 of Complement C3

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 1518 of Complement C3

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 C3 between cysteines 1511 and 1590 (1489 and 1568 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
2a73
Structure name
human complement component c3
Structure deposition date
2005-07-04
Thiol separation (Å)
10
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01024
Residue number A
1511
Residue number B
1590
Peptide name
Complement C3

Ligandability

Cysteine 1511 of Complement C3

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 1590 of Complement C3

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 C3 between cysteines 873 and 1511. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
PDB code
5o35
Structure name
structure of complement proteins complex
Structure deposition date
2017-05-23
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
17
% buried
nan
Peptide accession
P01024
Residue number A
873
Residue number B
1511
Peptide name
Complement C3

Ligandability

Cysteine 873 of Complement C3

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 1511 of Complement C3

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 C3 between cysteines 873 and 1518. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
23
PDB code
5fo8
Structure name
crystal structure of human complement c3b in complex with mcp (ccp1-4)
Structure deposition date
2015-11-18
Thiol separation (Å)
10
Half-sphere exposure sum ?
70
Minimum pKa ?
16
% buried
nan
Peptide accession
P01024
Residue number A
873
Residue number B
1518
Peptide name
Complement C3

Ligandability

Cysteine 873 of Complement C3

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 1518 of Complement C3

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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