Complement C5

Peptide B accession

Peptide A residue number

1159

Peptide B residue number

1101

Ligandability

Cysteine 1159 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

Cysteine 1101 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between two units of Complement C5 at cysteines 1159 and 1159. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

5i5k

Structure name

structure of complement c5 in complex with eculizumab

Structure deposition date

2016-02-15

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Complement C5

Peptide B name

Complement C5

Peptide A accession

Peptide B accession

Peptide A residue number

1159

Peptide B residue number

1159

Ligandability

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between two units of Complement C5 at cysteines 728 and 728. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

4p3a

Structure name

crystal structure of the mouse c5a anaphylatoxin

Structure deposition date

2014-03-06

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

Peptide A name

Complement C5

Peptide B name

Complement C5

Peptide A accession

Peptide B accession

Peptide A residue number

728

Peptide B residue number

728

Ligandability

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between two units of Complement C5 at cysteines 704 and 711 (27 and 34 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

3hqa

Structure name

crystal structure of human desarg-c5a

Structure deposition date

2009-06-05

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

nan

Peptide A name

Complement C5

Peptide B name

Complement C5

Peptide A accession

Peptide B accession

Peptide A residue number

704

Peptide B residue number

711

Ligandability

Cysteine 704 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

Cysteine 711 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between two units of Complement C5 at cysteines 728 and 702. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

4p3b

Structure name

crystal structure of the mouse c5a-desarg anaphylatoxin

Structure deposition date

2014-03-06

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Complement C5

Peptide B name

Complement C5

Peptide A accession

Peptide B accession

Peptide A residue number

728

Peptide B residue number

702

Ligandability

Cysteine 728 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

Cysteine 702 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between two units of Complement C5 at cysteines 711 and 699. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

4p39

Structure name

crystal structure of the human c5ar antagonist c5a-a8

Structure deposition date

2014-03-06

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Complement C5

Peptide B name

Complement C5

Peptide A accession

Peptide B accession

Peptide A residue number

711

Peptide B residue number

699

Ligandability

Cysteine 711 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

Cysteine 699 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between two units of Complement C5 at cysteines 731 and 731. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

4p39

Structure name

crystal structure of the human c5ar antagonist c5a-a8

Structure deposition date

2014-03-06

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Complement C5

Peptide B name

Complement C5

Peptide A accession

Peptide B accession

Peptide A residue number

731

Peptide B residue number

731

Ligandability

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between two units of Complement C5 at cysteines 702 and 702. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

4p3b

Structure name

crystal structure of the mouse c5a-desarg anaphylatoxin

Structure deposition date

2014-03-06

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Complement C5

Peptide B name

Complement C5

Peptide A accession

Peptide B accession

Peptide A residue number

702

Peptide B residue number

702

Ligandability

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between cysteine 1101 of Complement C5 and cysteine 59 of Complement inhibitor RaCI1 (1101 and 40 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

6rqj

Structure name

structure of human complement c5 complexed with tick inhibitors omci, raci1 and cirpt1

Structure deposition date

2019-05-15

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Complement C5

Peptide B name

Complement inhibitor RaCI1

Peptide A accession

Peptide B accession

A0A158RFT5

Peptide A residue number

1101

Peptide B residue number

Ligandability

Cysteine 1101 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

Cysteine 59 of Complement inhibitor RaCI1

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Complement C5 between cysteines 1520 and 1525.

Details

Redox score ?

PDB code

Structure name

crystal structure of complement c5 in complex with chemically synthesized k92 knob domain

Structure deposition date

2021-05-28

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

1520

Residue number B

1525

Peptide name

Complement C5

Ligandability

Cysteine 1520 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

Cysteine 1525 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Complement C5 between cysteines 1553 and 1676.

Details

Redox score ?

PDB code

Structure name

crystal structure of complement c5 in complex with chemically synthesized k92 knob domain

Structure deposition date

2021-05-28

Thiol separation (Å)

Half-sphere exposure sum ?

nan

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

1553

Residue number B

1676

Peptide name

Complement C5

Ligandability

Cysteine 1553 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

Cysteine 1676 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Complement C5 between cysteines 1654 and 1657.

Details

Redox score ?

PDB code

4e0s

Structure name

crystal structure of c5b-6

Structure deposition date

2012-03-05

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

1654

Residue number B

1657

Peptide name

Complement C5

Ligandability

Cysteine 1654 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

Cysteine 1657 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Complement C5 between cysteines 1532 and 1606.

Details

Redox score ?

PDB code

3prx

Structure name

structure of complement c5 in complex with cvf and ssl7

Structure deposition date

2010-11-30

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

1532

Residue number B

1606

Peptide name

Complement C5

Ligandability

Cysteine 1532 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

Cysteine 1606 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Complement C5 between cysteines 704 and 1676 (704 and 2006 respectively in this structure).

Details

Redox score ?

PDB code

5hcc

Structure name

ternary complex of human complement c5 with ornithodoros moubata omci and dermacentor andersoni raci3

Structure deposition date

2016-01-04

Thiol separation (Å)

Half-sphere exposure sum ?

nan

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

704

Residue number B

1676

Peptide name

Complement C5

Ligandability

Cysteine 704 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

Cysteine 1676 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Complement C5 between cysteines 634 and 1676 (634 and 669 respectively in this structure).

Details

Redox score ?

PDB code

7ad7

Structure name

crystal structure of human complement c5 in complex with the k8 bovine knob domain peptide

Structure deposition date

2020-09-14

Thiol separation (Å)

Half-sphere exposure sum ?

nan

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

634

Residue number B

1676

Peptide name

Complement C5

Ligandability

Cysteine 634 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

Cysteine 1676 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Complement C5 between cysteines 711 and 732.

Details

Redox score ?

PDB code

Structure name

structure of complement c5 in complex with ssl7

Structure deposition date

2009-11-09

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

711

Residue number B

732

Peptide name

Complement C5

Ligandability

Cysteine 711 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

Cysteine 732 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Complement C5 between cysteines 1375 and 1505.

Details

Redox score ?

PDB code

7ad7

Structure name

crystal structure of human complement c5 in complex with the k8 bovine knob domain peptide

Structure deposition date

2020-09-14

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

1375

Residue number B

1505

Peptide name

Complement C5

Ligandability

Cysteine 1375 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

Cysteine 1505 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Complement C5 between cysteines 698 and 724 (21 and 47 respectively in this structure).

Details

Redox score ?

PDB code

4uu9

Structure name

crystal structure of the human c5a in complex with medi7814 a neutralising antibody

Structure deposition date

2014-07-25

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

698

Residue number B

724

Peptide name

Complement C5

Ligandability

Cysteine 698 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

Cysteine 724 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Complement C5 between cysteines 866 and 1527.

Details

Redox score ?

PDB code

3cu7

Structure name

human complement component 5

Structure deposition date

2008-04-16

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

866

Residue number B

1527

Peptide name

Complement C5

Ligandability

Cysteine 866 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

Cysteine 1527 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Complement C5 between cysteines 1405 and 1474.

Details

Redox score ?

PDB code

Structure name

structure of complement c5 in complex with ssl7

Structure deposition date

2009-11-09

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

1405

Residue number B

1474

Peptide name

Complement C5

Ligandability

Cysteine 1405 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

Cysteine 1474 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Complement C5 between cysteines 634 and 669.

Details

Redox score ?

PDB code

7ad6

Structure name

crystal structure of human complement c5 in complex with the k92 bovine knob domain peptide

Structure deposition date

2020-09-14

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

634

Residue number B

669

Peptide name

Complement C5

Ligandability

Cysteine 634 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

Cysteine 669 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Complement C5 between cysteines 856 and 883.

Details

Redox score ?

PDB code

3prx

Structure name

structure of complement c5 in complex with cvf and ssl7

Structure deposition date

2010-11-30

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

856

Residue number B

883

Peptide name

Complement C5

Ligandability

Cysteine 856 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

Cysteine 883 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Complement C5 between cysteines 731 and 1676 (54 and 71 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

1cfa

Structure name

solution structure of a semi-synthetic c5a receptor antagonist at ph 5

Structure deposition date

1996-09-21

Thiol separation (Å)

Half-sphere exposure sum ?

nan

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

731

Residue number B

1676

Peptide name

Complement C5

Ligandability

Cysteine 731 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

Cysteine 1676 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Complement C5 between cysteines 699 and 1676 (22 and 71 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

1cfa

Structure name

solution structure of a semi-synthetic c5a receptor antagonist at ph 5

Structure deposition date

1996-09-21

Thiol separation (Å)

Half-sphere exposure sum ?

nan

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

699

Residue number B

1676

Peptide name

Complement C5

Ligandability

Cysteine 699 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

Cysteine 1676 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Complement C5 between cysteines 699 and 724. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

3km9

Structure name

structure of complement c5 in complex with the c-terminal beta-grasp domain of ssl7

Structure deposition date

2009-11-10

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

699

Residue number B

724

Peptide name

Complement C5

Ligandability

Cysteine 699 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

Cysteine 724 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Complement C5 between cysteines 1525 and 1532. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

Structure name

crystal structure of complement c5 in complex with chemically synthesized k92 knob domain

Structure deposition date

2021-05-28

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

1525

Residue number B

1532

Peptide name

Complement C5

Ligandability

Cysteine 1525 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

Cysteine 1532 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Complement C5 between cysteines 1520 and 1532. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

7ad6

Structure name

crystal structure of human complement c5 in complex with the k92 bovine knob domain peptide

Structure deposition date

2020-09-14

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

1520

Residue number B

1532

Peptide name

Complement C5

Ligandability

Cysteine 1520 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

Cysteine 1532 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Complement C5 between cysteines 1525 and 1527. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

Structure name

structure of complement c5 in complex with ssl7

Structure deposition date

2009-11-09

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

1525

Residue number B

1527

Peptide name

Complement C5

Ligandability

Cysteine 1525 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

Cysteine 1527 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Complement C5 between cysteines 1525 and 1606. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

Structure name

crystal structure of complement c5 in complex with chemically synthesized k92 knob domain

Structure deposition date

2021-05-28

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

1525

Residue number B

1606

Peptide name

Complement C5

Ligandability

Cysteine 1525 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

Cysteine 1606 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Complement C5 between cysteines 1520 and 1527. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

Structure name

structure of complement c5 in complex with ssl7

Structure deposition date

2009-11-09

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

1520

Residue number B

1527

Peptide name

Complement C5

Ligandability

Cysteine 1520 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

Cysteine 1527 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Complement C5 between cysteines 731 and 732. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

5hce

Structure name

ternary complex of human complement c5 with ornithodoros moubata omci and rhipicephalus appendiculatus raci1

Structure deposition date

2016-01-04

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

731

Residue number B

732

Peptide name

Complement C5

Ligandability

Cysteine 731 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

Cysteine 732 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Complement C5 between cysteines 1520 and 1606. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

5hcc

Structure name

ternary complex of human complement c5 with ornithodoros moubata omci and dermacentor andersoni raci3

Structure deposition date

2016-01-04

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

1520

Residue number B

1606

Peptide name

Complement C5

Ligandability

Cysteine 1520 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

Cysteine 1606 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Complement C5 between cysteines 866 and 1525. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

4e0s

Structure name

crystal structure of c5b-6

Structure deposition date

2012-03-05

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

866

Residue number B

1525

Peptide name

Complement C5

Ligandability

Cysteine 866 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

Cysteine 1525 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Complement C5 between cysteines 724 and 731. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

3km9

Structure name

structure of complement c5 in complex with the c-terminal beta-grasp domain of ssl7

Structure deposition date

2009-11-10

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

724

Residue number B

731

Peptide name

Complement C5

Ligandability

Cysteine 724 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

Cysteine 731 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Complement C5 between cysteines 698 and 699. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

5hce

Structure name

ternary complex of human complement c5 with ornithodoros moubata omci and rhipicephalus appendiculatus raci1

Structure deposition date

2016-01-04

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

698

Residue number B

699

Peptide name

Complement C5

Ligandability

Cysteine 698 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

Cysteine 699 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Complement C5 between cysteines 711 and 724 (34 and 47 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

1kjs

Structure name

nmr solution structure of c5a at ph 5

Structure deposition date

1997-01-09

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

711

Residue number B

724

Peptide name

Complement C5

Ligandability

Cysteine 711 of Complement C5

Not ligandable in the dataset of Vinogradova et al.

Cysteine 724 of Complement C5

Not ligandable in the dataset of Vinogradova et al.