Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

8B0H

2C9, C5b9-CD59 cryoEM structure

This is a non-PDB format compatible entry.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004866	molecular_function	endopeptidase inhibitor activity
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0006954	biological_process	inflammatory response
A	0006956	biological_process	complement activation
B	0005579	cellular_component	membrane attack complex
B	0006955	biological_process	immune response
C	0005579	cellular_component	membrane attack complex
C	0006955	biological_process	immune response
D	0005579	cellular_component	membrane attack complex
D	0006955	biological_process	immune response
E	0005579	cellular_component	membrane attack complex
E	0006955	biological_process	immune response
F	0005579	cellular_component	membrane attack complex
F	0006956	biological_process	complement activation
H	0005579	cellular_component	membrane attack complex
H	0006955	biological_process	immune response
I	0005579	cellular_component	membrane attack complex
I	0006955	biological_process	immune response

Functional Information from PROSITE/UniProt

site_id	PS00022
Number of Residues	12
Details	EGF_1 EGF-like domain signature 1. CqCrlGslGAaC

Chain	Residue	Details
E	CYS487-CYS498
D	CYS469-CYS480
C	CYS475-CYS486
H	CYS507-CYS518
B	CYS541-CYS552

site_id	PS00213
Number of Residues	14
Details	LIPOCALIN Lipocalin signature. NFDaqQFAGTWLLV

Chain	Residue	Details
F	ASN21-VAL34

site_id	PS00279
Number of Residues	12
Details	MACPF_1 Membrane attack complex/perforin (MACPF) domain signature. YakfindYGTHY

Chain	Residue	Details
E	TYR300-TYR311
D	TYR279-TYR290
C	TYR292-TYR303
H	TYR314-TYR325
B	TYR354-TYR365

site_id	PS00983
Number of Residues	44
Details	LY6_UPAR Ly-6 / u-PAR domain signature. QCYnCpnptad..Cktav....NCSsdfdaClitkaglqvynkcwkfeh......C

Chain	Residue	Details
G	GLN2-CYS45

site_id	PS01177
Number of Residues	35
Details	ANAPHYLATOXIN_1 Anaphylatoxin domain signature. CCydGacvnnde.TCEqraarisl.GprCikafte.CC

Chain	Residue	Details
A	CYS698-CYS732

site_id	PS01186
Number of Residues	16
Details	EGF_2 EGF-like domain signature 2. CvCkmPYecgpsldvC

Chain	Residue	Details
C	CYS713-CYS728
H	CYS505-CYS518

site_id	PS01209
Number of Residues	23
Details	LDLRA_1 LDL-receptor class A (LDLRA) domain signature. CLkrhlv.CNgdqDCldgsDEDd....C

Chain	Residue	Details
E	CYS78-CYS100
D	CYS79-CYS101
C	CYS96-CYS119
H	CYS91-CYS113
B	CYS151-CYS173

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Lipidation: {"description":"GPI-anchor amidated asparagine","evidences":[{"source":"PubMed","id":"17566972","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8276756","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"18780401","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8670172","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (Glc) (glycation) lysine","evidences":[{"source":"PubMed","id":"10805801","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
Details	Glycosylation: {"description":"O-linked (GalNAc...) threonine","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	216
Details	Domain: {"description":"TSP type-1 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00210","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	224
Details	Domain: {"description":"LDL-receptor class A","evidences":[{"source":"PROSITE-ProRule","id":"PRU00124","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	180
Details	Domain: {"description":"EGF-like"}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"21454577","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3OJY","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"21454577","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	12
Details	Glycosylation: {"description":"C-linked (Man) tryptophan","evidences":[{"source":"PubMed","id":"10551839","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30552328","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	146
Details	Domain: {"description":"TSP type-1 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00210","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	79
Details	Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	1
Details	Site: {"description":"Not glycosylated"}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	26
Details	Region: {"description":"Involved in the tick complement inhibitor CirpT1","evidences":[{"source":"PubMed","id":"31871188","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18536718","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21217642","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3CU7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3KLS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3KM9","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	118
Details	Domain: {"description":"Sushi 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00302","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI19
Number of Residues	147
Details	Region: {"description":"CCP 1"}

Chain

Residue

Details

site_id	SWS_FT_FI20
Number of Residues	12
Details	Compositional bias: {"description":"Acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

site_id	SWS_FT_FI21
Number of Residues	11
Details	Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

site_id	SWS_FT_FI22
Number of Residues	9
Details	Compositional bias: {"description":"Low complexity","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

site_id	SWS_FT_FI23
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"14760718","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI24
Number of Residues	10
Details	Glycosylation: {"description":"C-linked (Man) tryptophan; partial","evidences":[{"source":"PubMed","id":"10551839","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI25
Number of Residues	47
Details	Domain: {"description":"TSP type-1 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00210","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI26
Number of Residues	61
Details	Domain: {"description":"Sushi 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00302","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI27
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22500023","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4E0S","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI28
Number of Residues	2
Details	Glycosylation: {"description":"O-linked (Fuc...) threonine","evidences":[{"source":"PubMed","id":"22267737","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI29
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22267737","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI30
Number of Residues	106
Details	Domain: {"description":"TSP type-1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00210","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI31
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"14760718","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16263699","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19139490","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30552328","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"4055801","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI32
Number of Residues	7
Details	Transmembrane: {"description":"Beta stranded","evidences":[{"source":"PubMed","id":"30552328","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6H03","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6H04","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		Validation report (PDF)