4ROB

2.8A resolution structure of SRPN2 (K198C) from Anopheles gambiae

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004867	molecular_function	serine-type endopeptidase inhibitor activity
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0010951	biological_process	negative regulation of endopeptidase activity
A	0010955	biological_process	negative regulation of protein processing
A	0035009	biological_process	negative regulation of melanization defense response
A	0042832	biological_process	defense response to protozoan
A	0045087	biological_process	innate immune response
A	0045861	biological_process	negative regulation of proteolysis
B	0004867	molecular_function	serine-type endopeptidase inhibitor activity
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0005615	cellular_component	extracellular space
B	0010951	biological_process	negative regulation of endopeptidase activity
B	0010955	biological_process	negative regulation of protein processing
B	0035009	biological_process	negative regulation of melanization defense response
B	0042832	biological_process	defense response to protozoan
B	0045087	biological_process	innate immune response
B	0045861	biological_process	negative regulation of proteolysis
C	0004867	molecular_function	serine-type endopeptidase inhibitor activity
C	0005515	molecular_function	protein binding
C	0005576	cellular_component	extracellular region
C	0005615	cellular_component	extracellular space
C	0010951	biological_process	negative regulation of endopeptidase activity
C	0010955	biological_process	negative regulation of protein processing
C	0035009	biological_process	negative regulation of melanization defense response
C	0042832	biological_process	defense response to protozoan
C	0045087	biological_process	innate immune response
C	0045861	biological_process	negative regulation of proteolysis

Functional Information from PROSITE/UniProt

site_id	PS00284
Number of Residues	11
Details	SERPIN Serpins signature. FNANRPFIFfI

Chain	Residue	Details
A	PHE380-ILE390

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	SITE: Reactive bond => ECO:0000305|PubMed:25525260

Chain	Residue	Details
A	LYS371
B	LYS371
C	LYS371

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site_id	SWS_FT_FI2
Number of Residues	6
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498

Chain	Residue	Details
A	ASN294
A	ASN324
B	ASN294
B	ASN324
C	ASN294
C	ASN324

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