4DJZ

Catalytic fragment of masp-1 in complex with its specific inhibitor developed by directed evolution on sgci scaffold

Functional Information from GO Data

Chain	GOid	namespace	contents
B	0004252	molecular_function	serine-type endopeptidase activity
B	0006508	biological_process	proteolysis
D	0004252	molecular_function	serine-type endopeptidase activity
D	0006508	biological_process	proteolysis
H	0030414	molecular_function	peptidase inhibitor activity
I	0030414	molecular_function	peptidase inhibitor activity

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
B	VAL486-CYS491

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

Chain	Residue	Details
B	ASP640-VAL651

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	SITE: Reactive bond

Chain	Residue	Details
H	ARG33
I	ARG33
B	SER646
D	HIS490
D	ASP552
D	SER646

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site_id	SWS_FT_FI2
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490

Chain	Residue	Details
A	ASN385
C	ASN385

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site_id	SWS_FT_FI3
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11290788, ECO:0000269|PubMed:16335952

Chain	Residue	Details
A	ASN407
C	ASN407

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