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Complement component C7

Intramolecular
Cysteine 702 and cysteine 713
Cysteine 512 and cysteine 545
Cysteine 776 and cysteine 789
Cysteine 773 and cysteine 782
Cysteine 28 and cysteine 63
Cysteine 721 and cysteine 743
Cysteine 659 and cysteine 688
Cysteine 571 and cysteine 613
Cysteine 460 and cysteine 475
Cysteine 477 and cysteine 486
More...
Cysteine 39 and cysteine 73
Cysteine 805 and cysteine 838
Cysteine 715 and cysteine 750
Cysteine 791 and cysteine 825
Cysteine 728 and cysteine 763
Cysteine 797 and cysteine 818
Cysteine 337 and cysteine 353
Cysteine 457 and cysteine 473
Cysteine 103 and cysteine 119
Cysteine 631 and cysteine 673
Cysteine 91 and cysteine 109
Cysteine 455 and cysteine 505
Cysteine 85 and cysteine 96
Cysteine 599 and cysteine 626
Cysteine 42 and cysteine 79
Cysteine 433 and cysteine 560
Cysteine 128 and cysteine 165
Cysteine 523 and cysteine 535
Cysteine 475 and cysteine 486
Cysteine 773 and cysteine 776
Cysteine 776 and cysteine 782
Cysteine 789 and cysteine 825
Cysteine 789 and cysteine 791
Cysteine 460 and cysteine 486
Cysteine 782 and cysteine 789
Cysteine 460 and cysteine 477
Cysteine 773 and cysteine 789
Cysteine 475 and cysteine 477
Cysteine 776 and cysteine 825
Cysteine 457 and cysteine 475
A redox-regulated disulphide may form within Complement component C7 between cysteines 702 and 713.

Details

Redox score ?
90
PDB code
2wcy
Structure name
nmr solution structure of factor i-like modules of complement c7
Structure deposition date
2009-03-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
34
Minimum pKa ?
nan
% buried
nan
Peptide accession
P10643
Residue number A
702
Residue number B
713
Peptide name
Complement component C7

Ligandability

Cysteine 702 of Complement component C7

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 713 of Complement component C7

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 component C7 between cysteines 512 and 545.

Details

Redox score ?
88
PDB code
6h04
Structure name
closed conformation of the membrane attack complex
Structure deposition date
2018-07-06
Thiol separation (Å)
2
Half-sphere exposure sum ?
38
Minimum pKa ?
nan
% buried
nan
Peptide accession
P10643
Residue number A
512
Residue number B
545
Peptide name
Complement component C7

Ligandability

Cysteine 512 of Complement component C7

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 545 of Complement component C7

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 component C7 between cysteines 776 and 789.

Details

Redox score ?
88
PDB code
2wcy
Structure name
nmr solution structure of factor i-like modules of complement c7
Structure deposition date
2009-03-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P10643
Residue number A
776
Residue number B
789
Peptide name
Complement component C7

Ligandability

Cysteine 776 of Complement component C7

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 789 of Complement component C7

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 component C7 between cysteines 773 and 782.

Details

Redox score ?
87
PDB code
2wcy
Structure name
nmr solution structure of factor i-like modules of complement c7
Structure deposition date
2009-03-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
41
Minimum pKa ?
nan
% buried
nan
Peptide accession
P10643
Residue number A
773
Residue number B
782
Peptide name
Complement component C7

Ligandability

Cysteine 773 of Complement component C7

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 782 of Complement component C7

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 component C7 between cysteines 28 and 63.

Details

Redox score ?
87
PDB code
6h04
Structure name
closed conformation of the membrane attack complex
Structure deposition date
2018-07-06
Thiol separation (Å)
2
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P10643
Residue number A
28
Residue number B
63
Peptide name
Complement component C7

Ligandability

Cysteine 28 of Complement component C7

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 63 of Complement component C7

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 component C7 between cysteines 721 and 743.

Details

Redox score ?
87
PDB code
2wcy
Structure name
nmr solution structure of factor i-like modules of complement c7
Structure deposition date
2009-03-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P10643
Residue number A
721
Residue number B
743
Peptide name
Complement component C7

Ligandability

Cysteine 721 of Complement component C7

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 743 of Complement component C7

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 component C7 between cysteines 659 and 688 (637 and 666 respectively in this structure).

Details

Redox score ?
86
PDB code
7nyc
Structure name
cryoem structure of 3c9-smac
Structure deposition date
2021-03-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
P10643
Residue number A
659
Residue number B
688
Peptide name
Complement component C7

Ligandability

Cysteine 659 of Complement component C7

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 688 of Complement component C7

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 component C7 between cysteines 571 and 613.

Details

Redox score ?
86
PDB code
6h04
Structure name
closed conformation of the membrane attack complex
Structure deposition date
2018-07-06
Thiol separation (Å)
2
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P10643
Residue number A
571
Residue number B
613
Peptide name
Complement component C7

Ligandability

Cysteine 571 of Complement component C7

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 613 of Complement component C7

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 component C7 between cysteines 460 and 475 (438 and 453 respectively in this structure).

Details

Redox score ?
86
PDB code
7nyc
Structure name
cryoem structure of 3c9-smac
Structure deposition date
2021-03-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
P10643
Residue number A
460
Residue number B
475
Peptide name
Complement component C7

Ligandability

Cysteine 460 of Complement component C7

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 475 of Complement component C7

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 component C7 between cysteines 477 and 486 (455 and 464 respectively in this structure).

Details

Redox score ?
86
PDB code
7nyc
Structure name
cryoem structure of 3c9-smac
Structure deposition date
2021-03-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P10643
Residue number A
477
Residue number B
486
Peptide name
Complement component C7

Ligandability

Cysteine 477 of Complement component C7

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 486 of Complement component C7

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 component C7 between cysteines 39 and 73 (17 and 51 respectively in this structure).

Details

Redox score ?
85
PDB code
7nyc
Structure name
cryoem structure of 3c9-smac
Structure deposition date
2021-03-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
P10643
Residue number A
39
Residue number B
73
Peptide name
Complement component C7

Ligandability

Cysteine 39 of Complement component C7

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 73 of Complement component C7

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 component C7 between cysteines 805 and 838.

Details

Redox score ?
85
PDB code
2wcy
Structure name
nmr solution structure of factor i-like modules of complement c7
Structure deposition date
2009-03-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
P10643
Residue number A
805
Residue number B
838
Peptide name
Complement component C7

Ligandability

Cysteine 805 of Complement component C7

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 838 of Complement component C7

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 component C7 between cysteines 715 and 750.

Details

Redox score ?
85
PDB code
2wcy
Structure name
nmr solution structure of factor i-like modules of complement c7
Structure deposition date
2009-03-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
P10643
Residue number A
715
Residue number B
750
Peptide name
Complement component C7

Ligandability

Cysteine 715 of Complement component C7

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 750 of Complement component C7

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 component C7 between cysteines 791 and 825.

Details

Redox score ?
84
PDB code
2wcy
Structure name
nmr solution structure of factor i-like modules of complement c7
Structure deposition date
2009-03-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
P10643
Residue number A
791
Residue number B
825
Peptide name
Complement component C7

Ligandability

Cysteine 791 of Complement component C7

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 825 of Complement component C7

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 component C7 between cysteines 728 and 763.

Details

Redox score ?
84
PDB code
2wcy
Structure name
nmr solution structure of factor i-like modules of complement c7
Structure deposition date
2009-03-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P10643
Residue number A
728
Residue number B
763
Peptide name
Complement component C7

Ligandability

Cysteine 728 of Complement component C7

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 763 of Complement component C7

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 component C7 between cysteines 797 and 818.

Details

Redox score ?
84
PDB code
2wcy
Structure name
nmr solution structure of factor i-like modules of complement c7
Structure deposition date
2009-03-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P10643
Residue number A
797
Residue number B
818
Peptide name
Complement component C7

Ligandability

Cysteine 797 of Complement component C7

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 818 of Complement component C7

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 component C7 between cysteines 337 and 353 (315 and 331 respectively in this structure).

Details

Redox score ?
84
PDB code
7nyc
Structure name
cryoem structure of 3c9-smac
Structure deposition date
2021-03-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P10643
Residue number A
337
Residue number B
353
Peptide name
Complement component C7

Ligandability

Cysteine 337 of Complement component C7

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 353 of Complement component C7

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 component C7 between cysteines 457 and 473 (435 and 451 respectively in this structure).

Details

Redox score ?
84
PDB code
7nyc
Structure name
cryoem structure of 3c9-smac
Structure deposition date
2021-03-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
P10643
Residue number A
457
Residue number B
473
Peptide name
Complement component C7

Ligandability

Cysteine 457 of Complement component C7

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 473 of Complement component C7

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 component C7 between cysteines 103 and 119 (81 and 97 respectively in this structure).

Details

Redox score ?
84
PDB code
7nyc
Structure name
cryoem structure of 3c9-smac
Structure deposition date
2021-03-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P10643
Residue number A
103
Residue number B
119
Peptide name
Complement component C7

Ligandability

Cysteine 103 of Complement component C7

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 119 of Complement component C7

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 component C7 between cysteines 631 and 673 (609 and 651 respectively in this structure).

Details

Redox score ?
83
PDB code
7nyc
Structure name
cryoem structure of 3c9-smac
Structure deposition date
2021-03-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P10643
Residue number A
631
Residue number B
673
Peptide name
Complement component C7

Ligandability

Cysteine 631 of Complement component C7

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 673 of Complement component C7

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 component C7 between cysteines 91 and 109 (69 and 87 respectively in this structure).

Details

Redox score ?
82
PDB code
7nyc
Structure name
cryoem structure of 3c9-smac
Structure deposition date
2021-03-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
P10643
Residue number A
91
Residue number B
109
Peptide name
Complement component C7

Ligandability

Cysteine 91 of Complement component C7

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 109 of Complement component C7

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 component C7 between cysteines 455 and 505 (433 and 483 respectively in this structure).

Details

Redox score ?
82
PDB code
7nyc
Structure name
cryoem structure of 3c9-smac
Structure deposition date
2021-03-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P10643
Residue number A
455
Residue number B
505
Peptide name
Complement component C7

Ligandability

Cysteine 455 of Complement component C7

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 505 of Complement component C7

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 component C7 between cysteines 85 and 96 (63 and 74 respectively in this structure).

Details

Redox score ?
81
PDB code
7nyc
Structure name
cryoem structure of 3c9-smac
Structure deposition date
2021-03-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
P10643
Residue number A
85
Residue number B
96
Peptide name
Complement component C7

Ligandability

Cysteine 85 of Complement component C7

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 96 of Complement component C7

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 component C7 between cysteines 599 and 626.

Details

Redox score ?
81
PDB code
6h04
Structure name
closed conformation of the membrane attack complex
Structure deposition date
2018-07-06
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
9
% buried
15
Peptide accession
P10643
Residue number A
599
Residue number B
626
Peptide name
Complement component C7

Ligandability

Cysteine 599 of Complement component C7

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 626 of Complement component C7

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 component C7 between cysteines 42 and 79 (20 and 57 respectively in this structure).

Details

Redox score ?
81
PDB code
7nyc
Structure name
cryoem structure of 3c9-smac
Structure deposition date
2021-03-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P10643
Residue number A
42
Residue number B
79
Peptide name
Complement component C7

Ligandability

Cysteine 42 of Complement component C7

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 79 of Complement component C7

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 component C7 between cysteines 433 and 560 (411 and 538 respectively in this structure).

Details

Redox score ?
80
PDB code
7nyc
Structure name
cryoem structure of 3c9-smac
Structure deposition date
2021-03-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
P10643
Residue number A
433
Residue number B
560
Peptide name
Complement component C7

Ligandability

Cysteine 433 of Complement component C7

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 560 of Complement component C7

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 component C7 between cysteines 128 and 165.

Details

Redox score ?
79
PDB code
6h04
Structure name
closed conformation of the membrane attack complex
Structure deposition date
2018-07-06
Thiol separation (Å)
4
Half-sphere exposure sum ?
74
Minimum pKa ?
6
% buried
54
Peptide accession
P10643
Residue number A
128
Residue number B
165
Peptide name
Complement component C7

Ligandability

Cysteine 128 of Complement component C7

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 component C7

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 component C7 between cysteines 523 and 535.

Details

Redox score ?
74
PDB code
6h04
Structure name
closed conformation of the membrane attack complex
Structure deposition date
2018-07-06
Thiol separation (Å)
5
Half-sphere exposure sum ?
49
Minimum pKa ?
9
% buried
4
Peptide accession
P10643
Residue number A
523
Residue number B
535
Peptide name
Complement component C7

Ligandability

Cysteine 523 of Complement component C7

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 535 of Complement component C7

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 component C7 between cysteines 475 and 486 (453 and 464 respectively in this structure).

Details

Redox score ?
73
PDB code
7nyc
Structure name
cryoem structure of 3c9-smac
Structure deposition date
2021-03-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P10643
Residue number A
475
Residue number B
486
Peptide name
Complement component C7

Ligandability

Cysteine 475 of Complement component C7

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 486 of Complement component C7

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 component C7 between cysteines 773 and 776.

Details

Redox score ?
70
PDB code
2wcy
Structure name
nmr solution structure of factor i-like modules of complement c7
Structure deposition date
2009-03-17
Thiol separation (Å)
6
Half-sphere exposure sum ?
47
Minimum pKa ?
nan
% buried
2
Peptide accession
P10643
Residue number A
773
Residue number B
776
Peptide name
Complement component C7

Ligandability

Cysteine 773 of Complement component C7

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 776 of Complement component C7

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 component C7 between cysteines 776 and 782.

Details

Redox score ?
68
PDB code
2wcy
Structure name
nmr solution structure of factor i-like modules of complement c7
Structure deposition date
2009-03-17
Thiol separation (Å)
6
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
2
Peptide accession
P10643
Residue number A
776
Residue number B
782
Peptide name
Complement component C7

Ligandability

Cysteine 776 of Complement component C7

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 782 of Complement component C7

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 component C7 between cysteines 789 and 825.

Details

Redox score ?
67
PDB code
2wcy
Structure name
nmr solution structure of factor i-like modules of complement c7
Structure deposition date
2009-03-17
Thiol separation (Å)
6
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
11
Peptide accession
P10643
Residue number A
789
Residue number B
825
Peptide name
Complement component C7

Ligandability

Cysteine 789 of Complement component C7

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 825 of Complement component C7

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 component C7 between cysteines 789 and 791.

Details

Redox score ?
66
PDB code
2wcy
Structure name
nmr solution structure of factor i-like modules of complement c7
Structure deposition date
2009-03-17
Thiol separation (Å)
6
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
4
Peptide accession
P10643
Residue number A
789
Residue number B
791
Peptide name
Complement component C7

Ligandability

Cysteine 789 of Complement component C7

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 791 of Complement component C7

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 component C7 between cysteines 460 and 486.

Details

Redox score ?
65
PDB code
6h04
Structure name
closed conformation of the membrane attack complex
Structure deposition date
2018-07-06
Thiol separation (Å)
6
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P10643
Residue number A
460
Residue number B
486
Peptide name
Complement component C7

Ligandability

Cysteine 460 of Complement component C7

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 486 of Complement component C7

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 component C7 between cysteines 782 and 789.

Details

Redox score ?
63
PDB code
2wcy
Structure name
nmr solution structure of factor i-like modules of complement c7
Structure deposition date
2009-03-17
Thiol separation (Å)
7
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
1
Peptide accession
P10643
Residue number A
782
Residue number B
789
Peptide name
Complement component C7

Ligandability

Cysteine 782 of Complement component C7

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 789 of Complement component C7

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 component C7 between cysteines 460 and 477 (438 and 455 respectively in this structure).

Details

Redox score ?
63
PDB code
7nyc
Structure name
cryoem structure of 3c9-smac
Structure deposition date
2021-03-22
Thiol separation (Å)
6
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P10643
Residue number A
460
Residue number B
477
Peptide name
Complement component C7

Ligandability

Cysteine 460 of Complement component C7

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 477 of Complement component C7

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 component C7 between cysteines 773 and 789.

Details

Redox score ?
63
PDB code
2wcy
Structure name
nmr solution structure of factor i-like modules of complement c7
Structure deposition date
2009-03-17
Thiol separation (Å)
7
Half-sphere exposure sum ?
45
Minimum pKa ?
nan
% buried
1
Peptide accession
P10643
Residue number A
773
Residue number B
789
Peptide name
Complement component C7

Ligandability

Cysteine 773 of Complement component C7

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 789 of Complement component C7

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 component C7 between cysteines 475 and 477. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
6h04
Structure name
closed conformation of the membrane attack complex
Structure deposition date
2018-07-06
Thiol separation (Å)
7
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P10643
Residue number A
475
Residue number B
477
Peptide name
Complement component C7

Ligandability

Cysteine 475 of Complement component C7

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 477 of Complement component C7

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 component C7 between cysteines 776 and 825. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
2wcy
Structure name
nmr solution structure of factor i-like modules of complement c7
Structure deposition date
2009-03-17
Thiol separation (Å)
8
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
12
Peptide accession
P10643
Residue number A
776
Residue number B
825
Peptide name
Complement component C7

Ligandability

Cysteine 776 of Complement component C7

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 825 of Complement component C7

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 component C7 between cysteines 457 and 475 (435 and 453 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
7nyc
Structure name
cryoem structure of 3c9-smac
Structure deposition date
2021-03-22
Thiol separation (Å)
7
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
P10643
Residue number A
457
Residue number B
475
Peptide name
Complement component C7

Ligandability

Cysteine 457 of Complement component C7

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 475 of Complement component C7

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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