6F02

Crystal structure of human glycosylated kallistatin at 3.0 Angstrom resolution

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	0031089	cellular_component	platelet dense granule lumen
A	0070062	cellular_component	extracellular exosome
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	0031089	cellular_component	platelet dense granule lumen
C	0070062	cellular_component	extracellular exosome

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU397-ILE407

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	SITE: Reactive bond

Chain	Residue	Details
A	PHE388
C	PHE388

---

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

Chain	Residue	Details
A	ASN108
C	ASN108

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:16335952

Chain	Residue	Details
A	ASN157
C	ASN157

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490

Chain	Residue	Details
A	ASN238
C	ASN238

---