4IW4

Crystal structure of the serine protease domain of MASP-3 in complex with ecotin

Functional Information from GO Data

Chain	GOid	namespace	contents
C	0004867	molecular_function	serine-type endopeptidase inhibitor activity
C	0005515	molecular_function	protein binding
C	0006952	biological_process	defense response
C	0030288	cellular_component	outer membrane-bounded periplasmic space
C	0030414	molecular_function	peptidase inhibitor activity
C	0042597	cellular_component	periplasmic space
C	0042803	molecular_function	protein homodimerization activity
D	0004867	molecular_function	serine-type endopeptidase inhibitor activity
D	0005515	molecular_function	protein binding
D	0006952	biological_process	defense response
D	0030288	cellular_component	outer membrane-bounded periplasmic space
D	0030414	molecular_function	peptidase inhibitor activity
D	0042597	cellular_component	periplasmic space
D	0042803	molecular_function	protein homodimerization activity
E	0004252	molecular_function	serine-type endopeptidase activity
E	0006508	biological_process	proteolysis
F	0004252	molecular_function	serine-type endopeptidase activity
F	0006508	biological_process	proteolysis

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
E	ASP639-VAL650

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Site: {"description":"Reactive bond"}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	6
Details	Active site: {"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	4
Details	Glycosylation: {"description":"N-linked (GlcNAc) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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