Complement C4-A
Intermolecular
Cysteine 1394 and cysteine 1566 of Complement C4-B
Cysteine 1394 and cysteine 1566
Cysteine 567 and cysteine 820
Cysteine 876 and cysteine 1590 of Complement C4-B
Cysteine 876 and cysteine 1590
Cysteine 876 and cysteine 1588
Cysteine 876 and cysteine 1583
Cysteine 876 and cysteine 1595
Intramolecular
Cysteine 1595 and cysteine 1673
Cysteine 716 and cysteine 736
More...Cysteine 702 and cysteine 728
Cysteine 68 and cysteine 97
Cysteine 635 and cysteine 669
Cysteine 1718 and cysteine 1727
Cysteine 1583 and cysteine 1588
Cysteine 1618 and cysteine 1742
Cysteine 703 and cysteine 735
Cysteine 1471 and cysteine 1535
Cysteine 735 and cysteine 736
Cysteine 702 and cysteine 703
Cysteine 702 and cysteine 735
Cysteine 1588 and cysteine 1590
Cysteine 716 and cysteine 735
Cysteine 703 and cysteine 728
Cysteine 703 and cysteine 736
Cysteine 1583 and cysteine 1590
6ysq D 1394 F 1566
A redox-regulated disulphide may form between cysteine 1394 of Complement C4-A and cysteine 1566 of Complement C4-B.
Details
Redox score ?
86
PDB code
6ysq
Structure name
the hc4nb8 complement inhibitory nanobody in complex with c4b
Structure deposition date
2020-04-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide A name
Complement C4-A
Peptide B name
Complement C4-B
Peptide A accession
P0C0L4
Peptide B accession
P0C0L5
Peptide A residue number
1394
Peptide B residue number
1566
Ligandability
Cysteine 1394 of Complement C4-A
Cysteine 1566 of Complement C4-B
5jtw B 1394 C 1566
A redox-regulated disulphide may form between two units of Complement C4-A at cysteines 1394 and 1566.
Details
Redox score ?
84
PDB code
5jtw
Structure name
crystal structure of complement c4b re-refined using imdff
Structure deposition date
2016-05-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide A name
Complement C4-A
Peptide B name
Complement C4-A
Peptide A accession
P0C0L4
Peptide B accession
P0C0L4
Peptide A residue number
1394
Peptide B residue number
1566
Ligandability
Cysteine 1394 of Complement C4-A
Cysteine 1566 of Complement C4-A
6ysq A 567 C 820
A redox-regulated disulphide may form between two units of Complement C4-A at cysteines 567 and 820.
Details
Redox score ?
82
PDB code
6ysq
Structure name
the hc4nb8 complement inhibitory nanobody in complex with c4b
Structure deposition date
2020-04-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide A name
Complement C4-A
Peptide B name
Complement C4-A
Peptide A accession
P0C0L4
Peptide B accession
P0C0L4
Peptide A residue number
567
Peptide B residue number
820
Ligandability
Cysteine 567 of Complement C4-A
Cysteine 820 of Complement C4-A
6ysq C 876 E 1590
A redox-regulated disulphide may form between cysteine 876 of Complement C4-A and cysteine 1590 of Complement C4-B.
Details
Redox score ?
80
PDB code
6ysq
Structure name
the hc4nb8 complement inhibitory nanobody in complex with c4b
Structure deposition date
2020-04-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide A name
Complement C4-A
Peptide B name
Complement C4-B
Peptide A accession
P0C0L4
Peptide B accession
P0C0L5
Peptide A residue number
876
Peptide B residue number
1590
Ligandability
Cysteine 876 of Complement C4-A
Cysteine 1590 of Complement C4-B
5jpn B 876 C 1590
A redox-regulated disulphide may form between two units of Complement C4-A at cysteines 876 and 1590.
Details
Redox score ?
80
PDB code
5jpn
Structure name
structure of human complement c4 rebuilt using imdff
Structure deposition date
2016-05-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide A name
Complement C4-A
Peptide B name
Complement C4-A
Peptide A accession
P0C0L4
Peptide B accession
P0C0L4
Peptide A residue number
876
Peptide B residue number
1590
Ligandability
Cysteine 876 of Complement C4-A
Cysteine 1590 of Complement C4-A
5jpn B 876 C 1588
A redox-regulated disulphide may form between two units of Complement C4-A at cysteines 876 and 1588. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
5jpn
Structure name
structure of human complement c4 rebuilt using imdff
Structure deposition date
2016-05-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide A name
Complement C4-A
Peptide B name
Complement C4-A
Peptide A accession
P0C0L4
Peptide B accession
P0C0L4
Peptide A residue number
876
Peptide B residue number
1588
Ligandability
Cysteine 876 of Complement C4-A
Cysteine 1588 of Complement C4-A
5jpm E 876 F 1583
A redox-regulated disulphide may form between two units of Complement C4-A at cysteines 876 and 1583. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
5jpm
Structure name
structure of the complex of human complement c4 with masp-2 rebuilt using imdff
Structure deposition date
2016-05-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide A name
Complement C4-A
Peptide B name
Complement C4-A
Peptide A accession
P0C0L4
Peptide B accession
P0C0L4
Peptide A residue number
876
Peptide B residue number
1583
Ligandability
Cysteine 876 of Complement C4-A
Cysteine 1583 of Complement C4-A
5jpm B 876 C 1595
A redox-regulated disulphide may form between two units of Complement C4-A at cysteines 876 and 1595. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
5jpm
Structure name
structure of the complex of human complement c4 with masp-2 rebuilt using imdff
Structure deposition date
2016-05-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide A name
Complement C4-A
Peptide B name
Complement C4-A
Peptide A accession
P0C0L4
Peptide B accession
P0C0L4
Peptide A residue number
876
Peptide B residue number
1595
Ligandability
Cysteine 876 of Complement C4-A
Cysteine 1595 of Complement C4-A
4xam F 1595 F 1673
A redox-regulated disulphide may form within Complement C4-A between cysteines 1595 and 1673.
Details
Redox score ?
87
PDB code
4xam
Structure name
complement component c4b
Structure deposition date
2014-12-15
Thiol separation (Å)
2
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
P0C0L4
Residue number A
1595
Residue number B
1673
Peptide name
Complement C4-A
Ligandability
Cysteine 1595 of Complement C4-A
Cysteine 1673 of Complement C4-A
5jpn B 716 B 736
A redox-regulated disulphide may form within Complement C4-A between cysteines 716 and 736.
Details
Redox score ?
87
PDB code
5jpn
Structure name
structure of human complement c4 rebuilt using imdff
Structure deposition date
2016-05-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P0C0L4
Residue number A
716
Residue number B
736
Peptide name
Complement C4-A
Ligandability
Cysteine 716 of Complement C4-A
Cysteine 736 of Complement C4-A
5jpn B 702 B 728
A redox-regulated disulphide may form within Complement C4-A between cysteines 702 and 728.
Details
Redox score ?
85
PDB code
5jpn
Structure name
structure of human complement c4 rebuilt using imdff
Structure deposition date
2016-05-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P0C0L4
Residue number A
702
Residue number B
728
Peptide name
Complement C4-A
Ligandability
Cysteine 702 of Complement C4-A
Cysteine 728 of Complement C4-A
5jpn A 68 A 97
A redox-regulated disulphide may form within Complement C4-A between cysteines 68 and 97.
Details
Redox score ?
85
PDB code
5jpn
Structure name
structure of human complement c4 rebuilt using imdff
Structure deposition date
2016-05-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P0C0L4
Residue number A
68
Residue number B
97
Peptide name
Complement C4-A
Ligandability
Cysteine 68 of Complement C4-A
Cysteine 97 of Complement C4-A
5jpm D 635 D 669
A redox-regulated disulphide may form within Complement C4-A between cysteines 635 and 669.
Details
Redox score ?
84
PDB code
5jpm
Structure name
structure of the complex of human complement c4 with masp-2 rebuilt using imdff
Structure deposition date
2016-05-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
47
Minimum pKa ?
nan
% buried
nan
Peptide accession
P0C0L4
Residue number A
635
Residue number B
669
Peptide name
Complement C4-A
Ligandability
Cysteine 635 of Complement C4-A
Cysteine 669 of Complement C4-A
5jpm F 1718 F 1727
A redox-regulated disulphide may form within Complement C4-A between cysteines 1718 and 1727.
Details
Redox score ?
84
PDB code
5jpm
Structure name
structure of the complex of human complement c4 with masp-2 rebuilt using imdff
Structure deposition date
2016-05-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P0C0L4
Residue number A
1718
Residue number B
1727
Peptide name
Complement C4-A
Ligandability
Cysteine 1718 of Complement C4-A
Cysteine 1727 of Complement C4-A
5jpm F 1583 F 1588
A redox-regulated disulphide may form within Complement C4-A between cysteines 1583 and 1588.
Details
Redox score ?
84
PDB code
5jpm
Structure name
structure of the complex of human complement c4 with masp-2 rebuilt using imdff
Structure deposition date
2016-05-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P0C0L4
Residue number A
1583
Residue number B
1588
Peptide name
Complement C4-A
Ligandability
Cysteine 1583 of Complement C4-A
Cysteine 1588 of Complement C4-A
4fxg F 1618 F 1742
A redox-regulated disulphide may form within Complement C4-A between cysteines 1618 and 1742.
Details
Redox score ?
84
PDB code
4fxg
Structure name
complement c4 in complex with masp-2
Structure deposition date
2012-07-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
P0C0L4
Residue number A
1618
Residue number B
1742
Peptide name
Complement C4-A
Ligandability
Cysteine 1618 of Complement C4-A
Cysteine 1742 of Complement C4-A
5jpn B 703 B 735
A redox-regulated disulphide may form within Complement C4-A between cysteines 703 and 735.
Details
Redox score ?
82
PDB code
5jpn
Structure name
structure of human complement c4 rebuilt using imdff
Structure deposition date
2016-05-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P0C0L4
Residue number A
703
Residue number B
735
Peptide name
Complement C4-A
Ligandability
Cysteine 703 of Complement C4-A
Cysteine 735 of Complement C4-A
4xam F 1471 F 1535
A redox-regulated disulphide may form within Complement C4-A between cysteines 1471 and 1535.
Details
Redox score ?
80
PDB code
4xam
Structure name
complement component c4b
Structure deposition date
2014-12-15
Thiol separation (Å)
2
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P0C0L4
Residue number A
1471
Residue number B
1535
Peptide name
Complement C4-A
Ligandability
Cysteine 1471 of Complement C4-A
Cysteine 1535 of Complement C4-A
4fxk B 735 B 736
A redox-regulated disulphide may form within Complement C4-A between cysteines 735 and 736. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
4fxk
Structure name
human complement c4
Structure deposition date
2012-07-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P0C0L4
Residue number A
735
Residue number B
736
Peptide name
Complement C4-A
Ligandability
Cysteine 735 of Complement C4-A
Cysteine 736 of Complement C4-A
5jpn B 702 B 703
A redox-regulated disulphide may form within Complement C4-A between cysteines 702 and 703. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
5jpn
Structure name
structure of human complement c4 rebuilt using imdff
Structure deposition date
2016-05-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P0C0L4
Residue number A
702
Residue number B
703
Peptide name
Complement C4-A
Ligandability
Cysteine 702 of Complement C4-A
Cysteine 703 of Complement C4-A
4fxg B 702 B 735
A redox-regulated disulphide may form within Complement C4-A between cysteines 702 and 735. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
4fxg
Structure name
complement c4 in complex with masp-2
Structure deposition date
2012-07-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P0C0L4
Residue number A
702
Residue number B
735
Peptide name
Complement C4-A
Ligandability
Cysteine 702 of Complement C4-A
Cysteine 735 of Complement C4-A
4fxk C 1588 C 1590
A redox-regulated disulphide may form within Complement C4-A between cysteines 1588 and 1590. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
4fxk
Structure name
human complement c4
Structure deposition date
2012-07-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P0C0L4
Residue number A
1588
Residue number B
1590
Peptide name
Complement C4-A
Ligandability
Cysteine 1588 of Complement C4-A
Cysteine 1590 of Complement C4-A
5jpm E 716 E 735
A redox-regulated disulphide may form within Complement C4-A between cysteines 716 and 735. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
5jpm
Structure name
structure of the complex of human complement c4 with masp-2 rebuilt using imdff
Structure deposition date
2016-05-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
P0C0L4
Residue number A
716
Residue number B
735
Peptide name
Complement C4-A
Ligandability
Cysteine 716 of Complement C4-A
Cysteine 735 of Complement C4-A
5jpm E 703 E 728
A redox-regulated disulphide may form within Complement C4-A between cysteines 703 and 728. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
5jpm
Structure name
structure of the complex of human complement c4 with masp-2 rebuilt using imdff
Structure deposition date
2016-05-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P0C0L4
Residue number A
703
Residue number B
728
Peptide name
Complement C4-A
Ligandability
Cysteine 703 of Complement C4-A
Cysteine 728 of Complement C4-A
5jpm E 703 E 736
A redox-regulated disulphide may form within Complement C4-A between cysteines 703 and 736. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
36
PDB code
5jpm
Structure name
structure of the complex of human complement c4 with masp-2 rebuilt using imdff
Structure deposition date
2016-05-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
P0C0L4
Residue number A
703
Residue number B
736
Peptide name
Complement C4-A
Ligandability
Cysteine 703 of Complement C4-A
Cysteine 736 of Complement C4-A
5jtw F 1583 F 1590
A redox-regulated disulphide may form within Complement C4-A between cysteines 1583 and 1590. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
36
PDB code
5jtw
Structure name
crystal structure of complement c4b re-refined using imdff
Structure deposition date
2016-05-09
Thiol separation (Å)
10
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P0C0L4
Residue number A
1583
Residue number B
1590
Peptide name
Complement C4-A
Ligandability
Cysteine 1583 of Complement C4-A
Cysteine 1590 of Complement C4-A
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