Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2XWB

Crystal Structure of Complement C3b in complex with Factors B and D

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004866	molecular_function	endopeptidase inhibitor activity
B	0004866	molecular_function	endopeptidase inhibitor activity
B	0005576	cellular_component	extracellular region
B	0005615	cellular_component	extracellular space
C	0004866	molecular_function	endopeptidase inhibitor activity
D	0004866	molecular_function	endopeptidase inhibitor activity
D	0005576	cellular_component	extracellular region
D	0005615	cellular_component	extracellular space
F	0001848	molecular_function	complement binding
F	0002376	biological_process	immune system process
F	0004252	molecular_function	serine-type endopeptidase activity
F	0005515	molecular_function	protein binding
F	0005576	cellular_component	extracellular region
F	0005615	cellular_component	extracellular space
F	0005886	cellular_component	plasma membrane
F	0006508	biological_process	proteolysis
F	0006956	biological_process	complement activation
F	0006957	biological_process	complement activation, alternative pathway
F	0008233	molecular_function	peptidase activity
F	0008236	molecular_function	serine-type peptidase activity
F	0009617	biological_process	response to bacterium
F	0009986	cellular_component	cell surface
F	0016787	molecular_function	hydrolase activity
F	0045087	biological_process	innate immune response
F	0070062	cellular_component	extracellular exosome
F	0072562	cellular_component	blood microparticle
F	0106139	cellular_component	symbiont cell surface
H	0001848	molecular_function	complement binding
H	0002376	biological_process	immune system process
H	0004252	molecular_function	serine-type endopeptidase activity
H	0005515	molecular_function	protein binding
H	0005576	cellular_component	extracellular region
H	0005615	cellular_component	extracellular space
H	0005886	cellular_component	plasma membrane
H	0006508	biological_process	proteolysis
H	0006956	biological_process	complement activation
H	0006957	biological_process	complement activation, alternative pathway
H	0008233	molecular_function	peptidase activity
H	0008236	molecular_function	serine-type peptidase activity
H	0009617	biological_process	response to bacterium
H	0009986	cellular_component	cell surface
H	0016787	molecular_function	hydrolase activity
H	0045087	biological_process	innate immune response
H	0070062	cellular_component	extracellular exosome
H	0072562	cellular_component	blood microparticle
H	0106139	cellular_component	symbiont cell surface
I	0002376	biological_process	immune system process
I	0004252	molecular_function	serine-type endopeptidase activity
I	0005576	cellular_component	extracellular region
I	0005615	cellular_component	extracellular space
I	0006508	biological_process	proteolysis
I	0006956	biological_process	complement activation
I	0006957	biological_process	complement activation, alternative pathway
I	0008233	molecular_function	peptidase activity
I	0008236	molecular_function	serine-type peptidase activity
I	0016787	molecular_function	hydrolase activity
I	0031093	cellular_component	platelet alpha granule lumen
I	0031638	biological_process	zymogen activation
I	0034774	cellular_component	secretory granule lumen
I	0045087	biological_process	innate immune response
I	0051604	biological_process	protein maturation
I	0070062	cellular_component	extracellular exosome
I	1904813	cellular_component	ficolin-1-rich granule lumen
J	0002376	biological_process	immune system process
J	0004252	molecular_function	serine-type endopeptidase activity
J	0005576	cellular_component	extracellular region
J	0005615	cellular_component	extracellular space
J	0006508	biological_process	proteolysis
J	0006956	biological_process	complement activation
J	0006957	biological_process	complement activation, alternative pathway
J	0008233	molecular_function	peptidase activity
J	0008236	molecular_function	serine-type peptidase activity
J	0016787	molecular_function	hydrolase activity
J	0031093	cellular_component	platelet alpha granule lumen
J	0031638	biological_process	zymogen activation
J	0034774	cellular_component	secretory granule lumen
J	0045087	biological_process	innate immune response
J	0051604	biological_process	protein maturation
J	0070062	cellular_component	extracellular exosome
J	1904813	cellular_component	ficolin-1-rich granule lumen

Functional Information from PROSITE/UniProt

site_id	PS00134
Number of Residues	6
Details	TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LSAAHC

Chain	Residue	Details
I	LEU37-CYS42
F	LEU497-CYS502

site_id	PS00135
Number of Residues	12
Details	TRYPSIN_SER Serine proteases, trypsin family, serine active site. NTcrGDSGGPLI

Chain	Residue	Details
F	ASN668-ILE679

site_id	PS00477
Number of Residues	9
Details	ALPHA_2_MACROGLOBULIN Alpha-2-macroglobulin family thiolester region signature. PsGCGEEnM

Chain	Residue	Details
B	PRO985-MET993

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Site: {"description":"(Microbial infection) Cleavage; by S.pyogenes SpeB","evidences":[{"source":"PubMed","id":"18160402","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	14
Details	Modified residue: {"description":"Phosphoserine; by FAM20C","evidences":[{"source":"PubMed","id":"26091039","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12754519","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16263699","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17051150","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17684013","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2579379","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	32
Details	Peptide: {"description":"Complement C3f fragment","featureId":"PRO_0000005916","evidences":[{"source":"PubMed","id":"8376604","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	38
Details	Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	50
Details	Region: {"description":"Interaction with CFP/properdin","evidences":[{"source":"PubMed","id":"28264884","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31507604","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	6
Details	Site: {"description":"Cleavage; by factor I","evidences":[{"source":"PubMed","id":"28671664","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	2
Details	Site: {"description":"Coordinates Mg(2+) for interaction with Complement factor B Bb fragment (CFB)","evidences":[{"source":"PubMed","id":"28264884","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31507604","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"14760718","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17051150","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	4
Details	Cross-link: {"description":"Isoglutamyl cysteine thioester (Cys-Gln)","evidences":[{"source":"PubMed","id":"1577777","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6175959","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	130
Details	Domain: {"description":"Sushi 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00302","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	118
Details	Domain: {"description":"Sushi 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00302","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	114
Details	Domain: {"description":"Sushi 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00302","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	1014
Details	Domain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	6
Details	Active site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"10637221","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15016353","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1Q0P","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	4
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17310251","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6546754","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI19
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"17310251","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19574954","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6546754","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI20
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (Glc) (glycation) lysine","evidences":[{"source":"PubMed","id":"2006911","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI21
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17310251","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19503103","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19574954","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6546754","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2WIN","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI22
Number of Residues	8
Details	Region: {"description":"Self-inhibitor loop","evidences":[{"source":"PubMed","id":"10022823","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9753554","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI23
Number of Residues	2
Details	Active site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"7592653","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9753554","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI24
Number of Residues	2
Details	Active site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"7592653","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI25
Number of Residues	2
Details	Active site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"7592653","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21205667","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"22362762","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)