8B0G

2C9, C5b9-CD59 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
J	0005579	cellular_component	membrane attack complex
J	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. CiCpvGsqGLaC

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

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

Chain	Residue	Details
F	ASN21-VAL34

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

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

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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

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

Chain	Residue	Details
A	CYS698-CYS732

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site_id	PS01186
Number of Residues	14
Details	EGF_2 EGF-like domain signature 2. ClCacPFkfegia..C

Chain	Residue	Details
H	CYS505-CYS518
C	CYS713-CYS728

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

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

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	LIPID: GPI-anchor amidated asparagine => ECO:0000269|PubMed:17566972, ECO:0000269|PubMed:8276756

Chain	Residue	Details
G	ASN77
H	TYR314-GLY333
J	VAL293-TYR309
J	TYR314-GLY333
I	VAL293-TYR309
I	TYR314-GLY333

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:18780401, ECO:0000269|PubMed:8670172

Chain	Residue	Details
G	ASN18
B	TRP90
B	TRP568
B	TRP571
B	TRP574

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	CARBOHYD: N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:10805801

Chain	Residue	Details
G	LYS41
B	THR392
I	TRP27

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site_id	SWS_FT_FI4
Number of Residues	2
Details	CARBOHYD: O-linked (GalNAc...) threonine => ECO:0000305

Chain	Residue	Details
G	THR51
G	THR52
I	TRP30

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site_id	SWS_FT_FI5
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952

Chain	Residue	Details
B	ASN855
J	ASN256
I	ASN256

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site_id	SWS_FT_FI6
Number of Residues	3
Details	CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:4055801

Chain	Residue	Details
H	ASN394
J	ASN394
I	ASN394

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