2OAY

Crystal structure of latent human C1-inhibitor

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004867	molecular_function	serine-type endopeptidase inhibitor activity
A	0005615	cellular_component	extracellular space

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	PHE449-LEU459

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	SITE: Reactive bond for chymotrypsin

Chain	Residue	Details
A	ALA443

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site_id	SWS_FT_FI2
Number of Residues	1
Details	SITE: Reactive bond

Chain	Residue	Details
A	ARG444

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site_id	SWS_FT_FI3
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17488724, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:3756141

Chain	Residue	Details
A	ASN216

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site_id	SWS_FT_FI4
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:3756141

Chain	Residue	Details
A	ASN231

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site_id	SWS_FT_FI5
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine; in variant TA

Chain	Residue	Details
A	ASN250

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site_id	SWS_FT_FI6
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:3756141

Chain	Residue	Details
A	ASN330

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