1LQ8

Crystal structure of cleaved protein C 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
C	0004867	molecular_function	serine-type endopeptidase inhibitor activity
C	0005615	cellular_component	extracellular space
E	0004867	molecular_function	serine-type endopeptidase inhibitor activity
E	0005615	cellular_component	extracellular space
G	0004867	molecular_function	serine-type endopeptidase inhibitor activity
G	0005615	cellular_component	extracellular space

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
B	LEU363-ILE373

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	SITE: Reactive bond

Chain	Residue	Details
A	ARG354
C	ARG354
E	ARG354
G	ARG354

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site_id	SWS_FT_FI2
Number of Residues	4
Details	CARBOHYD: O-linked (GalNAc...) threonine => ECO:0000269|PubMed:21056543, ECO:0000269|PubMed:22171320

Chain	Residue	Details
A	THR20
C	THR20
E	THR20
G	THR20

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site_id	SWS_FT_FI3
Number of Residues	4
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:18467335

Chain	Residue	Details
A	ASN230
C	ASN230
E	ASN230
G	ASN230

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site_id	SWS_FT_FI4
Number of Residues	4
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12575940, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:18467335

Chain	Residue	Details
A	ASN243
C	ASN243
E	ASN243
G	ASN243

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site_id	SWS_FT_FI5
Number of Residues	4
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:18467335

Chain	Residue	Details
A	ASN319
C	ASN319
E	ASN319
G	ASN319

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